Journal articles: 'Protein nanoparticle'

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Dhar, Sunandan, Vishesh Sood, Garima Lohiya, Harini Deivendran, and Dhirendra S. Katti. "Role of Physicochemical Properties of Protein in Modulating the Nanoparticle-Bio Interface." Journal of Biomedical Nanotechnology 16, no. 8 (August 1, 2020): 1276–95. http://dx.doi.org/10.1166/jbn.2020.2958.

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Nanoparticles, on exposure to the biological milieu, tend to interact with macromolecules to form a biomolecular corona. The biomolecular corona confers a unique biological identity to nanoparticles, and its protein composition plays a deterministic role in the biological fate of nanoparticles. The physiological behavior of proteins stems from their physicochemical properties, including surface charge, hydrophobicity, and structural stability. However, there is insufficient understanding about the role of physicochemical properties of proteins in biomolecular corona formation. We hypothesized that the physicochemical properties of proteins would influence their interaction with nanoparticles and have a deterministic effect on nanoparticle-cell interactions. To test our hypothesis, we used model proteins from different structural classes to understand the effect of secondary structure elements of proteins on the nanoparticle-protein interface. Further, we modified the surface of proteins to study the role of protein surface characteristics in governing the nanoparticle-protein interface. For this study, we used mesoporous silica nanoparticles as a model nanoparticle system. We observed that the surface charge of proteins governs the nature of the primary interaction and the extent of subsequent secondary interactions causing structural rearrangements of the protein. We also observed that the secondary structural contents of proteins significantly affected both the extent of secondary interactions at the nanoparticle-protein interface and the dispersion state of the nanoparticle-protein complex. Further, we studied the interactions of different protein-coated nanoparticles with different cells (fibroblast, carcinoma, and macrophage). We observed that different cells internalized the nanoparticle-protein complex as a function of secondary structural components of the protein. The type of model protein had a significant effect on their internalization by macrophages. Overall, we observed that the physicochemical characteristics of proteins had a significant role in modulating the nanoparticle-bio-interface at the level of both biomolecular corona formation and nanoparticle internalization by cells.

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Lee, Hwankyu. "Molecular Modeling of Protein Corona Formation and Its Interactions with Nanoparticles and Cell Membranes for Nanomedicine Applications." Pharmaceutics 13, no. 5 (April 29, 2021): 637. http://dx.doi.org/10.3390/pharmaceutics13050637.

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The conformations and surface properties of nanoparticles have been modified to improve the efficiency of drug delivery. However, when nanoparticles flow through the bloodstream, they interact with various plasma proteins, leading to the formation of protein layers on the nanoparticle surface, called protein corona. Experiments have shown that protein corona modulates nanoparticle size, shape, and surface properties and, thus, influence the aggregation of nanoparticles and their interactions with cell membranes, which can increases or decreases the delivery efficiency. To complement these experimental findings and understand atomic-level phenomena that cannot be captured by experiments, molecular dynamics (MD) simulations have been performed for the past decade. Here, we aim to review the critical role of MD simulations to understand (1) the conformation, binding site, and strength of plasma proteins that are adsorbed onto nanoparticle surfaces, (2) the competitive adsorption and desorption of plasma proteins on nanoparticle surfaces, and (3) the interactions between protein-coated nanoparticles and cell membranes. MD simulations have successfully predicted the competitive binding and conformation of protein corona and its effect on the nanoparticle–nanoparticle and nanoparticle–membrane interactions. In particular, simulations have uncovered the mechanism regarding the competitive adsorption and desorption of plasma proteins, which helps to explain the Vroman effect. Overall, these findings indicate that simulations can now provide predications in excellent agreement with experimental observations as well as atomic-scale insights into protein corona formation and interactions.

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Lastra, Ruben O., Tatjana Paunesku, Barite Gutama, Filiberto Reyes, Josie François, Shelby Martinez, Lun Xin, et al. "Protein Binding Effects of Dopamine Coated Titanium Dioxide Shell Nanoparticles." Precision Nanomedicine 2, no. 4 (October 2, 2019): 393–438. http://dx.doi.org/10.33218/prnano2(4).190802.1.

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Non-targeted nanoparticles are capable of entering cells, passing through different subcellular compartments and accumulating on their surface a protein corona that changes over time. In this study, we used metal oxide nanoparticles with iron-oxide core covered with titanium dioxide shell (Fe3O4@TiO2), with a single layer of covalently bound dopamine covering the nanoparticle surface. Mixing nanoparticles with cellular protein isolates showed that these nanoparticles can form complexes with numerous cellular proteins. The addition of non-toxic quantities of nano-particles to HeLa cell culture resulted in their non-specific uptake and accumulation of protein corona on nanoparticle surface. TfRC, Hsp90 and PARP were followed as representative protein components of nanoparticle corona; each protein bound to nanoparticles with different affinity. The presence of nanoparticles in cells also mildly modulated gene expression on the level of mRNA. In conclusion, cells exposed to non-targeted nanoparticles show subtle but numerous changes that are consistent from one experiment to another.

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Cagliani, Roberta, Francesca Gatto, and Giuseppe Bardi. "Protein Adsorption: A Feasible Method for Nanoparticle Functionalization?" Materials 12, no. 12 (June 21, 2019): 1991. http://dx.doi.org/10.3390/ma12121991.

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Nanomaterials are now well-established components of many sectors of science and technology. Their sizes, structures, and chemical properties allow for the exploration of a vast range of potential applications and novel approaches in basic research. Biomedical applications, such as drug or gene delivery, often require the release of nanoparticles into the bloodstream, which is populated by blood cells and a plethora of small peptides, proteins, sugars, lipids, and complexes of all these molecules. Generally, in biological fluids, a nanoparticle’s surface is covered by different biomolecules, which regulate the interactions of nanoparticles with tissues and, eventually, their fate. The adsorption of molecules onto the nanomaterial is described as “corona” formation. Every blood particulate component can contribute to the creation of the corona, although small proteins represent the majority of the adsorbed chemical moieties. The precise rules of surface-protein adsorption remain unknown, although the surface charge and topography of the nanoparticle seem to discriminate the different coronas. We will describe examples of adsorption of specific biomolecules onto nanoparticles as one of the methods for natural surface functionalization, and highlight advantages and limitations. Our critical review of these topics may help to design appropriate nanomaterials for specific drug delivery.

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Levit, Shani L., Rebecca C. Walker, and Christina Tang. "Rapid, Single-Step Protein Encapsulation via Flash NanoPrecipitation." Polymers 11, no. 9 (August 27, 2019): 1406. http://dx.doi.org/10.3390/polym11091406.

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Flash NanoPrecipitation (FNP) is a rapid method for encapsulating hydrophobic materials in polymer nanoparticles with high loading capacity. Encapsulating biologics such as proteins remains a challenge due to their low hydrophobicity (logP < 6) and current methods require multiple processing steps. In this work, we report rapid, single-step protein encapsulation via FNP using bovine serum albumin (BSA) as a model protein. Nanoparticle formation involves complexation and precipitation of protein with tannic acid and stabilization with a cationic polyelectrolyte. Nanoparticle self-assembly is driven by hydrogen bonding and electrostatic interactions. Using this approach, high encapsulation efficiency (up to ~80%) of protein can be achieved. The resulting nanoparticles are stable at physiological pH and ionic strength. Overall, FNP is a rapid, efficient platform for encapsulating proteins for various applications.

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Yuan, Juan, Qing Quan Guo, Xiang Zhu He, and Yan Ping Liu. "Researching on the Adsorption of Protein on Gold Nanoparticles." Advanced Materials Research 194-196 (February 2011): 462–66. http://dx.doi.org/10.4028/www.scientific.net/amr.194-196.462.

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Because of their unique properties, gold nanoparticles(NPs) show a wide range of applications such as surface-enhanced raman characteristics, biological sensing, biomedical and other fields. Different initial concentrations of Bull Serum Albumin(BSA) and egg white lysozyme respectively react with different size of gold nanoparticles. The condition of adsorption is determined by spectrometry method, then the area of protein with different molecular mass on the surface of a gold nanoparticle is calculated. The results show that the larger particle size of a gold nanoparticle is, the more protein the surface a gold nanoparticle adsorbs; the smaller the molecular mass of protein is, the more protein is adsorbed by gold nanoparticles surface.

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Das, Anindita, Abhijit Chakrabarti, and Puspendu K. Das. "Suppression of protein aggregation by gold nanoparticles: a new way to store and transport proteins." RSC Advances 5, no. 48 (2015): 38558–70. http://dx.doi.org/10.1039/c4ra17026a.

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Hong, Seyoung, Dong Wook Choi, Hong Nam Kim, Chun Gwon Park, Wonhwa Lee, and Hee Ho Park. "Protein-Based Nanoparticles as Drug Delivery Systems." Pharmaceutics 12, no. 7 (June 29, 2020): 604. http://dx.doi.org/10.3390/pharmaceutics12070604.

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Nanoparticles have been extensively used as carriers for the delivery of chemicals and biomolecular drugs, such as anticancer drugs and therapeutic proteins. Natural biomolecules, such as proteins, are an attractive alternative to synthetic polymers commonly used in nanoparticle formulation because of their safety. In general, protein nanoparticles offer many advantages, such as biocompatibility and biodegradability. Moreover, the preparation of protein nanoparticles and the corresponding encapsulation process involved mild conditions without the use of toxic chemicals or organic solvents. Protein nanoparticles can be generated using proteins, such as fibroins, albumin, gelatin, gliadine, legumin, 30Kc19, lipoprotein, and ferritin proteins, and are prepared through emulsion, electrospray, and desolvation methods. This review introduces the proteins used and methods used in generating protein nanoparticles and compares the corresponding advantages and disadvantages of each.

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MONOPOLI, MARCO P., SHA WAN, FRANCESCA BALDELLI BOMBELLI, EUGENE MAHON, and KENNETH A. DAWSON. "COMPARISONS OF NANOPARTICLE PROTEIN CORONA COMPLEXES ISOLATED WITH DIFFERENT METHODS." Nano LIFE 03, no. 04 (December 2013): 1343004. http://dx.doi.org/10.1142/s1793984413430046.

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Nanoparticles, after incubation in biological fluids, adsorb several kinds of biomolecules like lipids, sugars and mainly proteins with high affinities for the nanoparticle surface and with long residence time, forming the so-called hard corona. The biological machinery, such as cellular barriers and membrane receptors can directly engage with the protein corona while the pristine surface may remain inaccessible. Here we isolate nanoparticles associated with strongly bound biomolecules from the unbound and loosely bound ones, by different approaches: centrifugation, size exclusion chromatography and magnetic isolation. The different separation methodologies, despite requiring diverse time and operating mechanisms, gave nanoparticle-hard corona complexes which were found to be remarkably similar in both dispersion properties and protein composition thus proving to be equally valid.

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Lohcharoenkal, Warangkana, Liying Wang, Yi Charlie Chen, and Yon Rojanasakul. "Protein Nanoparticles as Drug Delivery Carriers for Cancer Therapy." BioMed Research International 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/180549.

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Nanoparticles have increasingly been used for a variety of applications, most notably for the delivery of therapeutic and diagnostic agents. A large number of nanoparticle drug delivery systems have been developed for cancer treatment and various materials have been explored as drug delivery agents to improve the therapeutic efficacy and safety of anticancer drugs. Natural biomolecules such as proteins are an attractive alternative to synthetic polymers which are commonly used in drug formulations because of their safety. In general, protein nanoparticles offer a number of advantages including biocompatibility and biodegradability. They can be prepared under mild conditions without the use of toxic chemicals or organic solvents. Moreover, due to their defined primary structure, protein-based nanoparticles offer various possibilities for surface modifications including covalent attachment of drugs and targeting ligands. In this paper, we review the most significant advancements in protein nanoparticle technology and their use in drug delivery arena. We then examine the various sources of protein materials that have been used successfully for the construction of protein nanoparticles as well as their methods of preparation. Finally, we discuss the applications of protein nanoparticles in cancer therapy.

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Pakulska, Malgosia M., Irja Elliott Donaghue, Jaclyn M. Obermeyer, Anup Tuladhar, Christopher K. McLaughlin, Tyler N. Shendruk, and Molly S. Shoichet. "Encapsulation-free controlled release: Electrostatic adsorption eliminates the need for protein encapsulation in PLGA nanoparticles." Science Advances 2, no. 5 (May 2016): e1600519. http://dx.doi.org/10.1126/sciadv.1600519.

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Encapsulation of therapeutic molecules within polymer particles is a well-established method for achieving controlled release, yet challenges such as low loading, poor encapsulation efficiency, and loss of protein activity limit clinical translation. Despite this, the paradigm for the use of polymer particles in drug delivery has remained essentially unchanged for several decades. By taking advantage of the adsorption of protein therapeutics to poly(lactic-co-glycolic acid) (PLGA) nanoparticles, we demonstrate controlled release without encapsulation. In fact, we obtain identical, burst-free, extended-release profiles for three different protein therapeutics with and without encapsulation in PLGA nanoparticles embedded within a hydrogel. Using both positively and negatively charged proteins, we show that short-range electrostatic interactions between the proteins and the PLGA nanoparticles are the underlying mechanism for controlled release. Moreover, we demonstrate tunable release by modifying nanoparticle concentration, nanoparticle size, or environmental pH. These new insights obviate the need for encapsulation and offer promising, translatable strategies for a more effective delivery of therapeutic biomolecules.

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Lynch, Iseult, and Kenneth A. Dawson. "Protein-nanoparticle interactions." Nano Today 3, no. 1-2 (February 2008): 40–47. http://dx.doi.org/10.1016/s1748-0132(08)70014-8.

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Mao, Jinpeng, Yuexiang Lu, Ning Chang, Jiaoe Yang, Jiacheng Yang, Sichun Zhang, and Yueying Liu. "A nanoplasmonic probe as a triple channel colorimetric sensor array for protein discrimination." Analyst 141, no. 13 (2016): 4014–17. http://dx.doi.org/10.1039/c6an00302h.

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The salt-induced aggregation, nanoparticle regrowth and self-assembly behaviors of gold nanoparticles (AuNPs) and DNA conjugates could be changed after interaction with different proteins, generating various color changes and a unique fingerprint pattern for each protein.

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Uzhytchak, Mariia, Barbora Smolková, Mariia Lunova, Milan Jirsa, Adam Frtús, Šárka Kubinová, Alexandr Dejneka, and Oleg Lunov. "Iron Oxide Nanoparticle-Induced Autophagic Flux Is Regulated by Interplay between p53-mTOR Axis and Bcl-2 Signaling in Hepatic Cells." Cells 9, no. 4 (April 18, 2020): 1015. http://dx.doi.org/10.3390/cells9041015.

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Iron oxide-based nanoparticles have been repeatedly shown to affect lysosomal-mediated signaling. Recently, nanoparticles have demonstrated an ability to modulate autophagic flux via lysosome-dependent signaling. However, the precise underlying mechanisms of such modulation as well as the impact of cellular genetic background remain enigmatic. In this study, we investigated how lysosomal-mediated signaling is affected by iron oxide nanoparticle uptake in three distinct hepatic cell lines. We found that nanoparticle-induced lysosomal dysfunction alters sub-cellular localization of pmTOR and p53 proteins. Our data indicate that alterations in the sub-cellular localization of p53 protein induced by nanoparticle greatly affect the autophagic flux. We found that cells with high levels of Bcl-2 are insensitive to autophagy initiated by nanoparticles. Altogether, our data identify lysosomes as a central hub that control nanoparticle-mediated responses in hepatic cells. Our results provide an important fundamental background for the future development of targeted nanoparticle-based therapies.

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Park, Sung Jean. "Protein–Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles." International Journal of Nanomedicine Volume 15 (August 2020): 5783–802. http://dx.doi.org/10.2147/ijn.s254808.

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Bing, Jiang, Xu Xiao, David Julian McClements, Yuan Biao, and Cao Chongjiang. "Protein corona formation around inorganic nanoparticles: Food plant proteins-TiO2 nanoparticle interactions." Food Hydrocolloids 115 (June 2021): 106594. http://dx.doi.org/10.1016/j.foodhyd.2021.106594.

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Yang, Wen, Lin Wang, Evan M. Mettenbrink, Paul L. DeAngelis, and Stefan Wilhelm. "Nanoparticle Toxicology." Annual Review of Pharmacology and Toxicology 61, no. 1 (January 6, 2021): 269–89. http://dx.doi.org/10.1146/annurev-pharmtox-032320-110338.

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Nanoparticles from natural and anthropogenic sources are abundant in the environment, thus human exposure to nanoparticles is inevitable. Due to this constant exposure, it is critically important to understand the potential acute and chronic adverse effects that nanoparticles may cause to humans. In this review, we explore and highlight the current state of nanotoxicology research with a focus on mechanistic understanding of nanoparticle toxicity at organ, tissue, cell, and biomolecular levels. We discuss nanotoxicity mechanisms, including generation of reactive oxygen species, nanoparticle disintegration, modulation of cell signaling pathways, protein corona formation, and poly(ethylene glycol)-mediated immunogenicity. We conclude with a perspective on potential approaches to advance current understanding of nanoparticle toxicity. Such improved understanding may lead to mitigation strategies that could enable safe application of nanoparticles in humans. Advances in nanotoxicity research will ultimately inform efforts to establish standardized regulatory frameworks with the goal of fully exploiting the potential of nanotechnology while minimizing harm to humans.

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Yang, Ming-Hui, Shyng-Shiou Yuan, Ying-Fong Huang, Po-Chiao Lin, Chi-Yu Lu, Tze-Wen Chung, and Yu-Chang Tyan. "A Proteomic View to Characterize the Effect of Chitosan Nanoparticle to Hepatic Cells: Is Chitosan Nanoparticle an Enhancer of PI3K/AKT1/mTOR Pathway?" BioMed Research International 2014 (2014): 1–9. http://dx.doi.org/10.1155/2014/789591.

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Chitosan nanoparticle, a biocompatible material, was used as a potential drug delivery system widely. Our current investigation studies were the bioeffects of the chitosan nanoparticle uptake by liver cells. In this experiment, the characterizations of chitosan nanoparticles were measured by transmission electron microscopy and particle size analyzer. The average size of the chitosan nanoparticle was224.6±11.2 nm, and the average zeta potential was+14.08±0.7 mV. Moreover, using proteomic approaches to analyze the differential protein expression patterns resulted from the chitosan nanoparticle uptaken by HepG2 and CCL-13 cells identified several proteins involved in the PI3K/AKT1/mTOR pathway. Our experimental results have demonstrated that the chitosan nanoparticle may involve in the liver cancer cell metastasis and proliferation.

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Shao, Liqin, J. J. Diao, Zhipeng Tang, Song Liu, Sophie C. Shen, Jiankang Liu, Xianfeng Rui, Dapeng Yu, and Qing Zhao. "Gold nanoparticle wires for sensing DNA and DNA/protein interactions." Nanoscale 6, no. 8 (2014): 4089–95. http://dx.doi.org/10.1039/c3nr06560j.

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Gold nanoparticle wires are formed from nanoparticles by discontinuous Vertical Evaporation-driven Colloidal Deposition, and are shown to achieve a sensitive detection of DNA molecules and their interactions with proteins.

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Ishihara, Kazuhiko, Wei Xin Chen, and Yuuki Inoue. "Bioinspired and Multifunctional Phospholipid Polymer Nanoparticles." Advances in Science and Technology 102 (October 2016): 3–11. http://dx.doi.org/10.4028/www.scientific.net/ast.102.3.

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Photoreactive and cytocompatible polymer nanoparticles for immobilizing and photoinduced releasing proteins were prepared. A water-soluble and amphiphilic phospholipid polymer, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)-co-4-(4-(1-methacryloyloxyethyl)-2-methoxy-5-nitrophenoxy) butyric acid (PL)) (PMB-PL) was synthesized. The PMB-PL underwent a cleavage reaction at the PL unit by photoirradiation at a wavelength of 365 nm. Additionally, the PMB-PL took polymer aggregate in aqueous medium and was used to modify the surface of biodegradable poly (L-lactic acid) (PLA) nanoparticle as an emulsifier. The morphology of the PMB-PL/PLA nanoparticle was spherical and approximately 130 nm in diameter. The carboxylic acid group in the PL unit could be used for immobilization of proteins by covalent bonding. The bound proteins were released by a photoinduced cleavage reaction. Within 60 sec, up to 90% of the immobilized proteins were released by photoirradiation and activity of the protein released in the medium was maintained as well as that the original proteins before immobilization. Octa-arginine (R8) could promote internalization of the protein/PLA/PMB-PL nanoparticles into cells when the R8 was co-immobilized on the nanoparticles. After that, photoirradiation induced protein release from the nanoparticles and proteins distributed more evenly inside cells. From these results, we concluded that PMB-PL/PLA nanoparticles have the potential to be used as smart carriers to deliver proteins to biological systems, such as the inside of living cells.

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Nicoară, Raul, Maria Ilieș, Alina Uifălean, Cristina Adela Iuga, and Felicia Loghin. "Quantification of the PEGylated Gold Nanoparticles Protein Corona. Influence on Nanoparticle Size and Surface Chemistry." Applied Sciences 9, no. 22 (November 9, 2019): 4789. http://dx.doi.org/10.3390/app9224789.

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The interactions of nanoparticles with living organisms are driven by an interface called the protein corona. This interface is formed when nanoparticles are introduced in biological milieu and proteins are adsorbed at nanoparticles’ surfaces. Understanding the factors that are responsible for the formation and the composition of the protein corona could reveal mechanistic insights that are involved in the interaction of nanoparticles with biological structures. Multiple studies have qualitatively described the protein corona, but just a few have proposed quantification methods, especially for gold nanoparticles. Using bovine serum albumin conjugated with fluorescein-5-isothiocyanate as a model protein, we developed a fluorescent-based quantification method for gold nanoparticles’ protein coronas. The impact of nanoparticle size and surface chemistry was studied, and our research emphasizes that size and surface chemistry are determinant factors: Bigger nanoparticles and amino-modified surface chemistry are responsible for higher protein adsorption compared to smaller ones and carboxyl- or methoxy-modified surface chemistry. The proposed method can be used to complete the full picture of the interactions of nanoparticles with biological milieu and to describe the parameters which govern these interactions for the better development of nanomedicines.

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Yoshimura, Hideyuki. "Protein-assisted nanoparticle synthesis." Colloids and Surfaces A: Physicochemical and Engineering Aspects 282-283 (July 2006): 464–70. http://dx.doi.org/10.1016/j.colsurfa.2006.01.037.

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Alsharif, Shada A., David Power, Ian Rouse, and Vladimir Lobaskin. "In Silico Prediction of Protein Adsorption Energy on Titanium Dioxide and Gold Nanoparticles." Nanomaterials 10, no. 10 (October 4, 2020): 1967. http://dx.doi.org/10.3390/nano10101967.

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The free energy of adsorption of proteins onto nanoparticles offers an insight into the biological activity of these particles in the body, but calculating these energies is challenging at the atomistic resolution. In addition, structural information of the proteins may not be readily available. In this work, we demonstrate how information about adsorption affinity of proteins onto nanoparticles can be obtained from first principles with minimum experimental input. We use a multiscale model of protein–nanoparticle interaction to evaluate adsorption energies for a set of 59 human blood serum proteins on gold and titanium dioxide (anatase) nanoparticles of various sizes. For each protein, we compare the results for 3D structures derived from experiments to those predicted computationally from amino acid sequences using the I-TASSER methodology and software. Based on these calculations and 2D and 3D protein descriptors, we develop statistical models for predicting the binding energy of proteins, enabling the rapid characterization of the affinity of nanoparticles to a wide range of proteins.

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Shanwar, Samah, Liuen Liang, Andrey V. Nechaev, Daria K. Bausheva, Irina V. Balalaeva, Vladimir A. Vodeneev, Indrajit Roy, Andrei V. Zvyagin, and Evgenii L. Guryev. "Controlled Formation of a Protein Corona Composed of Denatured BSA on Upconversion Nanoparticles Improves Their Colloidal Stability." Materials 14, no. 7 (March 28, 2021): 1657. http://dx.doi.org/10.3390/ma14071657.

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In the natural fluidic environment of a biological system, nanoparticles swiftly adsorb plasma proteins on their surface forming a “protein corona”, which profoundly and often adversely affects their residence in the systemic circulation in vivo and their interaction with cells in vitro. It has been recognized that preformation of a protein corona under controlled conditions ameliorates the protein corona effects, including colloidal stability in serum solutions. We report on the investigation of the stabilizing effects of a denatured bovine serum albumin (dBSA) protein corona formed on the surface of upconversion nanoparticles (UCNPs). UCNPs were chosen as a nanoparticle model due to their unique photoluminescent properties suitable for background-free biological imaging and sensing. UCNP surface was modified with nitrosonium tetrafluoroborate (NOBF4) to render it hydrophilic. UCNP-NOBF4 nanoparticles were incubated in dBSA solution to form a dBSA corona followed up by lyophilization. As produced dBSA-UCNP-NOBF4 demonstrated high photoluminescence brightness, sustained colloidal stability after long-term storage and the reduced level of serum protein surface adsorption. These results show promise of dBSA-based nanoparticle pretreatment to improve the amiability to biological environments towards theranostic applications.

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Fitzkee, Nicholas C., Ailin Wang, Karen E. Woods, and Randika Perera. "How do Nanoparticle Size and Protein Charge Affect Gold Nanoparticle-Protein Interactions?" Biophysical Journal 110, no. 3 (February 2016): 529a—530a. http://dx.doi.org/10.1016/j.bpj.2015.11.2832.

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Di Ianni, Mauricio E., Germán A. Islan, Cecilia Y. Chain, Guillermo R. Castro, Alan Talevi, and María E. Vela. "Interaction of Solid Lipid Nanoparticles and Specific Proteins of the Corona Studied by Surface Plasmon Resonance." Journal of Nanomaterials 2017 (2017): 1–11. http://dx.doi.org/10.1155/2017/6509184.

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The applications of pharmaceutical and medical nanosystems are among the most intensively investigated fields in nanotechnology. A relevant point to be considered in the design and development of nanovehicles intended for medical use is the formation of the “protein corona” around the nanoparticle, that is, a complex biomolecular layer formed when the nanovehicle is exposed to biological fluids. The chemical nature of the protein corona determines the biological identity of the nanoparticle and influences, among others, the recognition of the nanocarrier by the mononuclear phagocytic system and, thus, its clearance from the blood. Recent works suggest that Surface Plasmon Resonance (SPR), extensively employed for the analysis of biomolecular interactions, can shed light on the formation of the protein corona and its interaction with the surroundings. The synthesis and characterization of solid lipid nanoparticles (SLN) coated with polymers of different chemical nature (e.g., polyvinyl alcohol, chitosans) are reported. The proof-of-concept for the use of SPR technique in characterizing protein-nanoparticle interactions of surface-immobilized proteins (immunoglobulin G and bovine serum albumin, both involved in the formation of the corona) subjected to flowing SLN is demonstrated for non-chitosan-coated nanoparticles. All assayed nanosystems show more preference for IgG than for BSA, such preference being more pronounced in the case of polyvinyl-alcohol-coated SLN.

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Thaxton, C. Shad, Nathaniel L. Rosi, and Chad A. Mirkin. "Optically and Chemically Encoded Nanoparticle Materials for DNA and Protein Detection." MRS Bulletin 30, no. 5 (May 2005): 376–80. http://dx.doi.org/10.1557/mrs2005.101.

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AbstractNanoscale materials are beginning to have an impact in the field of molecular diagnostics. In particular, gold nanoparticles surface-functionalized with DNA have garnered much recent interest. Due to the unusual optical and catalytic properties of gold nanoparticle labels, several distinct advantages for assay readout have been realized. This review focuses on the progress made in our group over the past seven years in the development of particle surface chemistry and ultrasensitive protein and nucleic acid assays based upon DNA-functionalized gold nanoparticles. For DNA targets, experiments demonstrate that assays based upon gold nanoparticle labels have enhanced target specificity and in certain cases the sensitivity of polymerase chain reaction (PCR), without the need for target amplification. For protein targets, similar experiments demonstrate that assays based upon gold nanoparticles are up to one million times more sensitive than conventional protein detection methods. Recent data using human samples demonstrate the utility of such assays.

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Zambre, Ajit, Nripen Chanda, Sudhirdas Prayaga, Rosana Almudhafar, Raghuraman Kannan, Anandhi Upendran, and Zahra Afrasiabi. "Gold Nanoparticle Based Immunostrip Assay Method for Detection of Protein-A." Applied Mechanics and Materials 229-231 (November 2012): 260–66. http://dx.doi.org/10.4028/www.scientific.net/amm.229-231.260.

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We have successfully developed gold nanoparticle based immunostrip assay to detect protein-A (PA). Rabbit polyclonal antibody IGg (αPA) that has affinity to PA was conjugated to gold nanoparticles (GNPs) and the gold nanoconjugate (αPA-GNP) was used to detect protein-A by simple immunostrip assay method. ELISA experiments were used to confirm the retention of binding affinity of antibody towards protein-A after conjugation with gold nanoparticles.

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Stewart, Madison, Marina Mulenos, London Steele, and Christie Sayes. "Differences among Unique Nanoparticle Protein Corona Constructs: A Case Study Using Data Analytics and Multi-Variant Visualization to Describe Physicochemical Characteristics." Applied Sciences 8, no. 12 (December 18, 2018): 2669. http://dx.doi.org/10.3390/app8122669.

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Gold nanoparticles (AuNPs) used in pharmaceutical treatments have been shown to effectively deliver a payload, such as an active pharmaceutical ingredient or image contrast agent, to targeted tissues in need of therapy or diagnostics while minimizing exposure, availability, and accumulation to surrounding biological compartments. Data sets collected in this field of study include some toxico- and pharmacodynamic properties (e.g., distribution and metabolism) but many studies lack information about adsorption of biological molecules or absorption into cells. When nanoparticles are suspended in blood serum, a protein corona cloud forms around its surface. The extent of the applications and implications of this formed cloud are unknown. Some researchers have speculated that the successful use of nanoparticles in pharmaceutical treatments relies on a comprehensive understanding of the protein corona composition. The work presented in this paper uses a suite of data analytics and multi-variant visualization techniques to elucidate particle-to-protein interactions at the molecular level. Through mass spectrometry analyses, corona proteins were identified through large and complex datasets. With such high-output analyses, complex datasets pose a challenge when visualizing and communicating nanoparticle-protein interactions. Thus, the creation of a streamlined visualization method is necessary. A series of user-friendly data informatics techniques were used to demonstrate the data flow of protein corona characteristics. Multi-variant heat maps, pie charts, tables, and three-dimensional regression analyses were used to improve results interpretation, facilitate an iterative data transfer process, and emphasize features of the nanoparticle-protein corona system that might be controllable. Data informatics successfully highlights the differences between protein corona compositions and how they relate to nanoparticle surface charge.

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Chinnathambi, Shanmugavel, Nobutaka Hanagata, Tomohiko Yamazaki, and Naoto Shirahata. "Nano-Bio Interaction between Blood Plasma Proteins and Water-Soluble Silicon Quantum Dots with Enabled Cellular Uptake and Minimal Cytotoxicity." Nanomaterials 10, no. 11 (November 13, 2020): 2250. http://dx.doi.org/10.3390/nano10112250.

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A better understanding of the compatibility of water-soluble semiconductor quantum dots (QDs) upon contact with the bloodstream is important for biological applications, including biomarkers working in the first therapeutic spectral window for deep tissue imaging. Herein, we investigated the conformational changes of blood plasma proteins during the interaction with near-infrared light-emitting nanoparticles, consisting of Pluronic F127 shells and cores comprised of assembled silicon QDs terminated with decane monolayers. Albumin and transferrin have high quenching constants and form a hard protein corona on the nanoparticle. In contrast, fibrinogen has low quenching constants and forms a soft protein corona. A circular dichroism (CD) spectrometric study investigates changes in the protein’s secondary and tertiary structures with incremental changes in the nanoparticle concentrations. As expected, the addition of nanoparticles causes the denaturation of the plasma proteins. However, it is noteworthy that the conformational recovery phenomena are observed for fibrinogen and transferrin, suggesting that the nanoparticle does not influence the ordered structure of proteins in the bloodstream. In addition, we observed enabled cellular uptake (NIH3T3 Fibroblasts) and minimal cytotoxicity using different cell lines (HeLa, A549, and NIH3T3). This study offers a basis to design QDs without altering the biomacromolecule’s original conformation with enabled cellular uptake with minimal cytotoxicity.

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Scaletti, Federica, Joseph Hardie, Yi-Wei Lee, David C. Luther, Moumita Ray, and Vincent M. Rotello. "Protein delivery into cells using inorganic nanoparticle–protein supramolecular assemblies." Chemical Society Reviews 47, no. 10 (2018): 3421–32. http://dx.doi.org/10.1039/c8cs00008e.

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Marichal, Laurent, Géraldine Klein, Jean Armengaud, Yves Boulard, Stéphane Chédin, Jean Labarre, Serge Pin, Jean-Philippe Renault, and Jean-Christophe Aude. "Protein Corona Composition of Silica Nanoparticles in Complex Media: Nanoparticle Size does not Matter." Nanomaterials 10, no. 2 (January 29, 2020): 240. http://dx.doi.org/10.3390/nano10020240.

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Biomolecules, and particularly proteins, bind on nanoparticle (NP) surfaces to form the so-called protein corona. It is accepted that the corona drives the biological distribution and toxicity of NPs. Here, the corona composition and structure were studied using silica nanoparticles (SiNPs) of different sizes interacting with soluble yeast protein extracts. Adsorption isotherms showed that the amount of adsorbed proteins varied greatly upon NP size with large NPs having more adsorbed proteins per surface unit. The protein corona composition was studied using a large-scale label-free proteomic approach, combined with statistical and regression analyses. Most of the proteins adsorbed on the NPs were the same, regardless of the size of the NPs. To go beyond, the protein physicochemical parameters relevant for the adsorption were studied: electrostatic interactions and disordered regions are the main driving forces for the adsorption on SiNPs but polypeptide sequence length seems to be an important factor as well. This article demonstrates that curvature effects exhibited using model proteins are not determining factors for the corona composition on SiNPs, when dealing with complex biological media.

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Tavanti, Francesco, and Maria Cristina Menziani. "Computational Insight on the Interaction of Common Blood Proteins with Gold Nanoparticles." International Journal of Molecular Sciences 22, no. 16 (August 13, 2021): 8722. http://dx.doi.org/10.3390/ijms22168722.

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Protein interactions with engineered gold nanoparticles (AuNPs) and the consequent formation of the protein corona are very relevant and poorly understood biological phenomena. The nanoparticle coverage affects protein binding modalities, and the adsorbed protein sites influence interactions with other macromolecules and cells. Here, we studied four common blood proteins, i.e., hemoglobin, serum albumin, α1-antiproteinase, and complement C3, interacting with AuNPs covered by hydrophobic 11-mercapto-1-undecanesulfonate (MUS). We use Molecular Dynamics and the Martini coarse−grained model to gain quantitative insight into the kinetics of the interaction, the physico-chemical characteristics of the binding site, and the nanoparticle adsorption capacity. Results show that proteins bind to MUS−capped AuNPs through strong hydrophobic interactions and that they adapt to the AuNP surfaces to maximize the contact surface, but no dramatic change in the secondary structure of the proteins is observed. We suggest a new method to calculate the maximum adsorption capacity of capped AuNPs based on the effective surface covered by each protein, which better represents the realistic behavior of these systems.

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Begarani, Filippo, Domenico Cassano, Eleonora Margheritis, Roberto Marotta, Francesco Cardarelli, and Valerio Voliani. "Silica-Based Nanoparticles for Protein Encapsulation and Delivery." Nanomaterials 8, no. 11 (November 1, 2018): 886. http://dx.doi.org/10.3390/nano8110886.

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Although conceptually obvious, the effective delivery of proteins in therapeutic applications is far from being a routine practice. The major limitation is the conservation of protein physicochemical identity during the transport to the target site. In this regard, nanoparticle-based systems offer new intriguing possibilities, provided that (i) the harsh and denaturating conditions typically used for nanoparticle synthesis are avoided or mitigated; and (ii) nanoparticle biocompatibility and degradation (for protein release) are optimized. Here, we tackle these issues by starting from a nanoparticle architecture already tested for small chemical compounds. In particular, silica-shielded liposomes are produced and loaded with a test protein (i.e., Green Fluorescent Protein) in an aqueous environment. We demonstrate promising results concerning protein encapsulation, protection during intracellular trafficking and final release triggered by nanoparticle degradations in acidic organelles. We believe this proof of principle may open new applications and developments for targeted and efficient protein delivery.

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Sánchez-García, L., N. Serna, M. Mattanovich, P. Cazzanelli, A. Sánchez-Chardi, O. Conchillo-Solé, F. Cortés, et al. "The fusogenic peptide HA2 impairs selectivity of CXCR4-targeted protein nanoparticles." Chemical Communications 53, no. 33 (2017): 4565–68. http://dx.doi.org/10.1039/c6cc09900a.

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We demonstrate here that the genetic incorporation of the fusogenic peptide HA2 to a CXCR4-targeted protein nanoparticle dramatically reduces the specificity of the interaction between nanoparticles and cell receptor.

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Qin, Dilan, Xiaoxiao He, Kemin Wang, Xiaojun Julia Zhao, Weihong Tan, and Jiyun Chen. "Fluorescent Nanoparticle-Based Indirect Immunofluorescence Microscopy for Detection ofMycobacterium tuberculosis." Journal of Biomedicine and Biotechnology 2007 (2007): 1–9. http://dx.doi.org/10.1155/2007/89364.

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A method of fluorescent nanoparticle-based indirect immunofluorescence microscopy (FNP-IIFM) was developed for the rapid detection ofMycobacterium tuberculosis. An anti-Mycobacterium tuberculosisantibody was used as primary antibody to recognizeMycobacterium tuberculosis, and then an antibody binding protein (Protein A) labeled with Tris(2,2-bipyridyl)dichlororuthenium(II) hexahydrate (RuBpy)-doped silica nanoparticles was used to generate fluorescent signal for microscopic examination. Prior to the detection, Protein A was immobilized on RuBpy-doped silica nanoparticles with a coverage of∼5.1×102molecules/nanoparticle. With this method,Mycobacterium tuberculosisin bacterial mixture as well as in spiked sputum was detected. The use of the fluorescent nanoparticles reveals amplified signal intensity and higher photostability than the direct use of conventional fluorescent dye as label. Our preliminary studies have demonstrated the potential application of the FNP-IIFM method for rapid detection ofMycobacterium tuberculosisin clinical samples.

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Lizoń, Anna, Joanna Tisończyk, Marta Gajewska, and Ryszard Drożdż. "Silver Nanoparticles as a Tool for the Study of Spontaneous Aggregation of Immunoglobulin Monoclonal Free Light Chains." International Journal of Molecular Sciences 22, no. 18 (September 8, 2021): 9703. http://dx.doi.org/10.3390/ijms22189703.

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Some misfolded proteins, e.g., immunoglobulin monoclonal free light chains (FLC), tend to form fibrils. Protein deposits in tissue may lead to amyloidosis and dysfunction of different organs. There is currently no technique allowing for the identification of FLC that are prone to aggregate. The development of such a method would enable the early selection of patients at high risk of developing amyloidosis. The aim of this study was to investigate whether silver nanoparticles (AgNPs) could be a useful tool to study the process of aggregation of FLC and their susceptibility to form the protein deposits. Mixtures of AgNPs and urine samples from patients with multiple myeloma were prepared. To evaluate the aggregation process of nanoparticles coated with proteins, UV-visible spectroscopy, transmission electron microscopy, and the original laser light scattering method were used. It has been shown that some clones of FLC spontaneously triggered aggregation of the nanoparticles, while in the presence of others, the nanoparticle solution became hyperstable. This is probably due to the structure of the chains themselves, unique protein-AgNPs interactions and perhaps correlates with the tendency of some FLC clones to form deposits. Nanoparticle technology has proven to be helpful in identifying clones of immunoglobulin FLC that tend to aggregate.

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Sit, Izaac, Haibin Wu, and Vicki H. Grassian. "Environmental Aspects of Oxide Nanoparticles: Probing Oxide Nanoparticle Surface Processes Under Different Environmental Conditions." Annual Review of Analytical Chemistry 14, no. 1 (June 5, 2021): 489–514. http://dx.doi.org/10.1146/annurev-anchem-091420-092928.

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Surface chemistry affects the physiochemical properties of nanoparticles in a variety of ways. Therefore, there is great interest in understanding how nanoparticle surfaces evolve under different environmental conditions of pH and temperature. Here, we discuss the use of vibrational spectroscopy as a tool that allows for in situ observations of oxide nanoparticle surfaces and their evolution due to different surface processes. We highlight oxide nanoparticle surface chemistry, either engineered anthropogenic or naturally occurring geochemical nanoparticles, in complex media, with a focus on the impact of ( a) pH on adsorption, intermolecular interactions, and conformational changes; ( b) surface coatings and coadsorbates on protein adsorption kinetics and protein conformation; ( c) surface adsorption on the temperature dependence of protein structure phase changes; and ( d) the use of two-dimensional correlation spectroscopy to analyze spectroscopic results for complex systems. An outlook of the field and remaining challenges is also presented.

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Maffre, Pauline, Karin Nienhaus, Faheem Amin, Wolfgang J. Parak, and G. Ulrich Nienhaus. "Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy." Beilstein Journal of Nanotechnology 2 (July 12, 2011): 374–83. http://dx.doi.org/10.3762/bjnano.2.43.

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Using dual-focus fluorescence correlation spectroscopy, we have analyzed the adsorption of three human blood serum proteins, namely serum albumin, apolipoprotein A-I and apolipoprotein E4, onto polymer-coated, fluorescently labeled FePt nanoparticles (~12 nm diameter) carrying negatively charged carboxyl groups on their surface. For all three proteins, a step-wise increase in hydrodynamic radius with protein concentration was observed, strongly suggesting the formation of protein monolayers that enclose the nanoparticles. Consistent with this interpretation, the absolute increase in hydrodynamic radius can be correlated with the molecular shapes of the proteins known from X-ray crystallography and solution experiments, indicating that the proteins bind on the nanoparticles in specific orientations. The equilibrium dissociation coefficients, measuring the affinity of the proteins to the nanoparticles, were observed to differ by almost four orders of magnitude. These variations can be understood in terms of the electrostatic properties of the proteins. From structure-based calculations of the surface potentials, positively charged patches of different extents can be revealed, through which the proteins interact electrostatically with the negatively charged nanoparticle surfaces.

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Eigenheer, Richard, Erick R. Castellanos, Meagan Y. Nakamoto, Kyle T. Gerner, Alyssa M. Lampe, and Korin E. Wheeler. "Silver nanoparticle protein corona composition compared across engineered particle properties and environmentally relevant reaction conditions." Environ. Sci.: Nano 1, no. 3 (2014): 238–47. http://dx.doi.org/10.1039/c4en00002a.

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Yang, Guang, Yue Lu, Hunter N. Bomba, and Zhen Gu. "Cysteine-rich Proteins for Drug Delivery and Diagnosis." Current Medicinal Chemistry 26, no. 8 (May 16, 2019): 1377–88. http://dx.doi.org/10.2174/0929867324666170920163156.

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An emerging focus in nanomedicine is the exploration of multifunctional nanocomposite materials that integrate stimuli-responsive, therapeutic, and/or diagnostic functions. In this effort, cysteine-rich proteins have drawn considerable attention as a versatile platform due to their good biodegradability, biocompatibility, and ease of chemical modification. This review surveys cysteine-rich protein-based biomedical materials, including protein-metal nanohybrids, gold nanoparticle-protein agglomerates, protein-based nanoparticles, and hydrogels, with an emphasis on their preparation methods, especially those based on the cysteine residue-related reactions. Their applications in tumor-targeted drug delivery and diagnostics are highlighted.

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Chong, Wei Lim, Koollawat Chupradit, Sek Peng Chin, Mai Mai Khoo, Sook Mei Khor, Chatchai Tayapiwatana, Piyarat Nimmanpipug, Weeraya Thongkum, and Vannajan Sanghiran Lee. "Protein-Protein Interactions: Insight from Molecular Dynamics Simulations and Nanoparticle Tracking Analysis." Molecules 26, no. 18 (September 20, 2021): 5696. http://dx.doi.org/10.3390/molecules26185696.

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Protein-protein interaction plays an essential role in almost all cellular processes and biological functions. Coupling molecular dynamics (MD) simulations and nanoparticle tracking analysis (NTA) assay offered a simple, rapid, and direct approach in monitoring the protein-protein binding process and predicting the binding affinity. Our case study of designed ankyrin repeats proteins (DARPins)—AnkGAG1D4 and the single point mutated AnkGAG1D4-Y56A for HIV-1 capsid protein (CA) were investigated. As reported, AnkGAG1D4 bound with CA for inhibitory activity; however, it lost its inhibitory strength when tyrosine at residue 56 AnkGAG1D4, the most key residue was replaced by alanine (AnkGAG1D4-Y56A). Through NTA, the binding of DARPins and CA was measured by monitoring the increment of the hydrodynamic radius of the AnkGAG1D4-gold conjugated nanoparticles (AnkGAG1D4-GNP) and AnkGAG1D4-Y56A-GNP upon interaction with CA in buffer solution. The size of the AnkGAG1D4-GNP increased when it interacted with CA but not AnkGAG1D4-Y56A-GNP. In addition, a much higher binding free energy (∆GB) of AnkGAG1D4-Y56A (−31 kcal/mol) obtained from MD further suggested affinity for CA completely reduced compared to AnkGAG1D4 (−60 kcal/mol). The possible mechanism of the protein-protein binding was explored in detail by decomposing the binding free energy for crucial residues identification and hydrogen bond analysis.

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SEKIGUCHI, M., K. OIKAWA, M. NAKAHARA, Y. INABA, T. MAEDA, A. MATSUI, and H. ISHIZAKI. "Preparation of Cu nanoparticle colloid from a Cu ion solution by using protein surfactant." MRS Advances 4, no. 24 (2019): 1393–98. http://dx.doi.org/10.1557/adv.2019.72.

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ABSTRACTIn this paper, a colloidal solution of copper nanoparticles was prepared from a Cu ion aqueous solution with the protein casein surfactant by a liquid phase reduction method at low temperature below 373K. For the casein concentration ranging from 6g/L to 75g/L, the formation of copper nanoparticle colloid were observed. As a result, the peak was observed at the ranging of 450 to 650 nm corresponding to the copper nanoparticle colloid plasmon absorption. As the surfactant concentration increases, the absorption spectrum tends to blue-shift and the particle diameter decreases. Thus, it indicated that the optical property and particle diameter of copper nanoparticle colloidal solution will be controlled by the protein casein surfactant concentration.

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Guzmán-Soto, Irene, Mary Omole, Emilio I. Alarcon, and Christopher D. McTiernan. "Lipoic acid capped silver nanoparticles: a facile route to covalent protein capping and oxidative stability within biological systems." RSC Advances 10, no. 54 (2020): 32953–58. http://dx.doi.org/10.1039/d0ra07080g.

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Covalent attachment of human serum albumin protein to the surface of spherical lipoic acid capped silver nanoparticles results in the generation of stable nanoparticle–protein hybrids with well defined surface composition.

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Matsuzaki, Yuka, Rina Maruta, Keiko Takaki, Eiji Kotani, Yasuko Kato, Ryoichi Yoshimura, Yasuhisa Endo, et al. "Sustained Neurotrophin Release from Protein Nanoparticles Mediated by Matrix Metalloproteinases Induces the Alignment and Differentiation of Nerve Cells." Biomolecules 9, no. 10 (September 20, 2019): 510. http://dx.doi.org/10.3390/biom9100510.

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The spatial and temporal availability of cytokines, and the microenvironments this creates, is critical to tissue development and homeostasis. Creating concentration gradients in vitro using soluble proteins is challenging as they do not provide a self-sustainable source. To mimic the sustained cytokine secretion seen in vivo from the extracellular matrix (ECM), we encapsulated a cargo protein into insect virus-derived proteins to form nanoparticle co-crystals and studied the release of this cargo protein mediated by matrix metalloproteinase-2 (MMP-2) and MMP-8. Specifically, when nerve growth factor (NGF), a neurotrophin, was encapsulated into nanoparticles, its release was promoted by MMPs secreted by a PC12 neuronal cell line. When these NGF nanoparticles were spotted onto a cover slip to create a uniform circular field, movement and alignment of PC12 cells via their extended axons along the periphery of the NGF nanoparticle field was observed. Neural cell differentiation was confirmed by the expression of specific markers of tau, neurofilament, and GAP-43. Connections between the extended axons and the growth cones were also observed, and expression of connexin 43 was consistent with the formation of gap junctions. Extensions and connection of very fine filopodia occurred between growth cones. Our studies indicate that crystalline protein nanoparticles can be utilized to generate a highly stable cytokine gradient microenvironment that regulates the alignment and differentiation of nerve cells. This technique greatly simplifies the creation of protein concentration gradients and may lead to therapies for neuronal injuries and disease.

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Ahmed, Marwa Aly, Júlia Erdőssy, and Viola Horváth. "The Role of the Initiator System in the Synthesis of Acidic Multifunctional Nanoparticles Designed for Molecular Imprinting of Proteins." Periodica Polytechnica Chemical Engineering 65, no. 1 (August 24, 2020): 28–41. http://dx.doi.org/10.3311/ppch.15414.

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Multifunctional nanoparticles have been shown earlier to bind certain proteins with high affinity and the binding affinity could be enhanced by molecular imprinting of the target protein. In this work different initiator systems were used and compared during the synthesis of poly (N-isopropylacrylamide-co-acrylic acid-co-N-tert-butylacrylamide) nanoparticles with respect to their future applicability in molecular imprinting of lysozyme. The decomposition of ammonium persulfate initiator was initiated either thermally at 60 °C or by using redox activators, namely tetramethylethylenediamine or sodium bisulfite at low temperatures. Morphology differences in the resulting nanoparticles have been revealed using scanning electron microscopy and dynamic light scattering. During polymerization the conversion of each monomer was followed in time. Striking differences were demonstrated in the incorporation rate of acrylic acid between the tetramethylethylenediamine catalyzed initiation and the other systems. This led to a completely different nanoparticle microstructure the consequence of which was the distinctly lower lysozyme binding affinity. On the contrary, the use of sodium bisulfite activation resulted in similar nanoparticle structural homogeneity and protein binding affinity as the thermal initiation.

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Fruehauf, Krista R., Tae Il Kim, Edward L. Nelson, Joseph P. Patterson, Szu-Wen Wang, and Kenneth J. Shea. "Metabolite Responsive Nanoparticle–Protein Complex." Biomacromolecules 20, no. 7 (May 22, 2019): 2703–12. http://dx.doi.org/10.1021/acs.biomac.9b00470.

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Bassett, David C., Liam M. Grover, Frank A. Müller, Marc D. McKee, and Jake E. Barralet. "Serum Protein Controlled Nanoparticle Synthesis." Advanced Functional Materials 21, no. 15 (May 24, 2011): 2968–77. http://dx.doi.org/10.1002/adfm.201100320.

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Padalkar, S., J. D. Hulleman, S. M. Kim, J. C. Rochet, E. A. Stach, and L. A. Stanciu. "Protein-templated semiconductor nanoparticle chains." Nanotechnology 19, no. 27 (May 28, 2008): 275602. http://dx.doi.org/10.1088/0957-4484/19/27/275602.

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You, Chang-Cheng, Mrinmoy De, and Vincent M. Rotello. "Monolayer-protected nanoparticle–protein interactions." Current Opinion in Chemical Biology 9, no. 6 (December 2005): 639–46. http://dx.doi.org/10.1016/j.cbpa.2005.09.012.

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Journal articles on the topic 'Protein nanoparticle'

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