Relevant bibliographies by topics / Protein nanoparticle

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
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Academic literature on the topic 'Protein nanoparticle'

Author: Grafiati
Published: 4 June 2021
Last updated: 15 February 2022

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Journal articles on the topic "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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Dissertations / Theses on the topic "Protein nanoparticle"

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Haghighat, Manesh Mohamad Javad Haghighat. "Effects of the Nanoparticle Protein Corona on Nanoparticle-Cell Membrane Interactions." Ohio University / OhioLINK, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1597967288027448.

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Lucon, Janice Elizabeth. "Development of protein nanoparticle based composite materials." Diss., Montana State University, 2013. http://etd.lib.montana.edu/etd/2013/lucon/LuconJ0513.pdf.

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Inspired by the core-shell composite structures found in nature, a range of protein based composites have been developed. These materials were made using synthetic approaches, which utilized the native protein architecture as an initiation point and size constrained reaction vessel for the piecewise formation of the second material. In the first illustration of this approach, a protein-P t composite was formed, where the protein cage has been modified to include a metal binding moiety for improved synthesis of metallic P t nanoclusters, which were shown to be an active H &#8322; catalyst. This composite was analyzed by native mass spectrometry to determine the number of P t ions bound prior to mineralization and to measure the distribution of species after mineralization, which provided a unique view into the mineralization process. The second illustration was a material synthesized using the cage-like protein architecture as an internal guiding synthetic scaffold for the formation of a coordination polymer core inside the protein cage. The construction of this coordination polymer was unusual in that unlike normal coordination polymer synthesis, coordination of the metal preceded formation the ditopic ligands, which were afterwards completed using azide-alkyne click chemistry. Finally, a collection of protein-polymer composites were developed, which utilized a living radical polymerization method, atom transfer radical polymerization, to form internal polymer cores. By labeling one of these protein-polymer constructs with a Gd based MRI contrast agent a material with vastly improved relaxivity was made. The development of each of these three types of composites served to improve our understanding of the natural systems, from which they are derived, and provide a basis for further development of advanced multicomponent nanomaterials. 'Co-authored by Md Joynal Abedin, Masaki Uchida, Lars Liepold, Craig C. Jolley, Mark Young, Trevor Douglas, Shefah Qazi, Gregory J. Bedwell, Ben LaFrance, and Peter E. Prevelige, Jr.'
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Pham, Tuan Anh [Verfasser]. "Protein assisted nanoparticle assembly and protein-nanocomposite fabrication / Tuan Anh Pham." Konstanz : Bibliothek der Universität Konstanz, 2016. http://d-nb.info/1119707870/34.

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Gallagher, Jane. "Protein nanoparticle conjugates for use in bioanalytical applications." Thesis, University of Strathclyde, 2011. http://oleg.lib.strath.ac.uk:80/R/?func=dbin-jump-full&object_id=17065.

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Maury, Pascale Anne. "Fabrication of nanoparticle and protein nanostructures using nanoimprint lithography." Enschede : University of Twente [Host], 2007. http://doc.utwente.nl/57701.

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Wright, Kimberley Elizabeth. "Engineering of a specific binding site for protein labelling with luminescent lanthanide coated nanoparticles : a study of protein labelling and nanoparticle-peptide interactions." Thesis, University of Birmingham, 2015. http://etheses.bham.ac.uk//id/eprint/5576/.

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The work presented in this thesis investigates the use of new luminescent lanthanide complexes, both free and bound to the surface of gold nanoparticles, for protein labelling. Lanthanide complexes were shown to maintain their luminescence properties when conjugated to proteins and one complex also demonstrated participation in Förster resonance energy transfer when conjugated to a protein in an appropriate system. Furthermore, it was found that bovine serum albumin can act as a vehicle to transport luminescent lanthanide complexes into two human cell lines. Lanthanide complexes were then used to coat 13 nm gold nanoparticles for protein labelling within cells. The aim was to find a peptide sequence to preferentially bind to gold nanoparticles which could be expressed as part of a protein of interest, acting as a binding site within the cell. The interaction of peptides with gold nanoparticles was examined using several methods and, of the sequences tested, CCPGCC was found to have the highest affinity for the nanoparticles. This peptide was expressed in HeLa cells as part of green fluorescent protein. Co-localisation of the nanoparticles with the protein in cells could not be established through fluorescence microscopy, however, cell lysis revealed green fluorescence protein associated with nanoparticle aggregate.
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Fernandez, Maxence. "Auto-assemblage de nanoparticules métalliques et semi-conductrices dirigé par reconnaissance entre protéines artificielles." Thesis, Rennes 1, 2019. http://www.theses.fr/2019REN1S129.

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L’auto-assemblage de nanoparticules dirigé par des biomolécules constitue une approche prometteuse pour la mise au point de nanomatériaux structurés présentant des propriétés optiques collectives originales. L’objet de cette thèse concerne l’auto-assemblage de nanoparticules métalliques et semi-conductrices dirigé par des protéines artificielles appelées α-Repeat. Dans cette optique, des nanocristaux semi-conducteurs (CdSe/ZnS ou CdSe/CdS) et des nanoparticules d’or sphériques ou anisotropes ont été préparés. Ces nanoparticules ont été fonctionnalisées avec des ligands peptidiques PEGylés, qui leur confère une stabilité colloïdale satisfaisante tout en conservant leurs propriétés optiques. Une stratégie de fonctionnalisation basée sur des étiquettes d’affinité poly-cystéine et poly-histidine a permis de greffer les protéines sur la surface des nanoparticules inorganiques. Les nanoparticules ainsi fonctionnalisées avec les protéines artificielles ont ensuite été utilisées pour l’auto-assemblage de nanoparticules semi-conductrices et l’auto-assemblage hybride entre des nanoparticules semi-conductrices et des nanoparticules métalliques. L’étude structurale des ensembles obtenus a montré, dans certains cas, une interdistance bien définie et inférieure à 10 nm. Finalement, l’étude des propriétés optiques a révélé des transferts d’énergie non radiatifs entre nanoparticules semi-conductrices et nanoparticules métalliques, qui témoignent d’interactions exciton—plasmon très fortes induites par l’auto-assemblage
Nanoparticles self-assembly driven by biomolecules is a promising approach for developing nanostructured materials with new optical properties. The purpose of this work is the self-assembly of metal and semiconductor nanoparticles directed by artificial proteins called α-Repeat. For this purpose, semiconductor nanocrystals (CdSe/ZnS or CdSe/CdS) and spherical or anisotropic gold nanoparticles have been prepared. These nanoparticles have been functionalized with PEGylated peptide ligands providing them adequate colloidal stability while maintaining their optical properties. A functionalization strategy based on polycysteine and poly-histidine tags has allowed the proteins to be grafted onto the surface of inorganic nanoparticles. Nanoparticles functionalized with artificial proteins were then used for the self-assembly of semiconductor nanoparticles and hybrid self-assembly between semiconductor nanoparticles and metal nanoparticles. The structure study of self-assembled nanostructures has shown, in some cases, a very well defined sub-10 nm interparticle distance. Finally, the study of optical properties revealed very strong exciton-plasmon interactions induced by self-assembly. This self-assembling process strongly affected the emission properties of the semiconductor nanoparticles in hybrid ensembles
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Davidson, Patricia Marie L. "Langmuir films and nanoparticle applications of a spider silk protein analog." Thesis, McGill University, 2006. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=100794.

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A synthetic analog of a spider silk protein (M4) was studied. Langmuir films were made and an inflexion in the isotherm indicated conformational changes upon compression. Deposition onto solid substrates was most successful using a hydrophobic substrate and the Langmuir-Schaeffer method. AFM was used to image the surface, which was mesh like and did not show any indication of order.
Gold nanoparticles were produced in the presence of the protein and protein solutions were added to read made nanoparticles for the purpose of displacing the weak ligands present. CD measurements were performed on the protein solutions to study its conformation. Nanoparticle size information was obtained from TEM images. DLS was used to determine if the protein was affected by the addition of the gold nanoparticles. Precipitation of the protein was shown not to affect the nanoparticles.
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Zhang, Xiaolu. "NANOPARTICLE BEHAVIOR IN BIOLOGICAL GELS AND BIOFLUIDS: THE IMPACT OF INTERACTIONS WITH CHARGED BIOGELS AND THE FORMATION OF PROTEIN CORONAS ON NANOPARTICLES." UKnowledge, 2015. http://uknowledge.uky.edu/chemistry_etds/57.

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With the rapid growth of nanotechnology, situations where nanomaterials will interact with biological systems will unquestionably grow. Therefore, it is increasingly understood that interactions between nanomaterials and biological environments will play an essential role in nanomedicine. Biological polymer networks, including mucus and the extracellular matrix, serve as a filter for the exchange of molecules and nanoparticles. Such polymer networks are complex and heterogeneous hydrogel environments that regulate transport processes through finely tuned particle-network interactions. In chapters 3 and 4, we investigate the role of electrostatics on the basic mechanisms governing the diffusion of charged molecules inside model polymer networks by using fluorescence correlation spectroscopy (FCS). In chapter 3, we show that particle transport of charged probe molecules in charged hydrogels is highly asymmetric and that the filtering capability of the gel is sensitive to the solution ionic strength. Brownian dynamics simulations are in quantitative agreement with our experimental result. In chapter 4, we focus on hyperbranched cationic dendrimer macromolecules (polyamidoamine, PAMAM) which differ from probes in size, charge density and chain flexibilities. Our results show PAMAM has strongly reduced mobility in like charge gels and greatly enhanced apparent diffusivity in oppositely charged gels. Further studies with salt suggest that the oppositely charged polymer network acts as a giant counterion enhancing the mobility of PAMAM by changing its conformation to a more compacted state. Due to their large surface areas, nanomaterials in biological fluids are modified by adsorption of biomolecules, mainly proteins, to form so called “protein coronas”. These coronas ultimately define the biological identity of the nanoparticles and dictate the interactions of cells with the protein-NP complex. We have studied the adsorption of human transferrin and bovine serum albumin on the surface of sulfonated polystyrene nanoparticle. In chapter 5, we show the formation of multi-layered protein coronas and compare to established adsorption models. In addition we followed for the first time the protein binding kinetics as a function of pH and salt. Through these studies, we aim to gain quantitative knowledge of the dynamic rearrangement of proteins on engineered nanomaterials.
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Giraudon--Colas, Gaël. "Caractérisation multiéchelle d'assemblages d'hémoglobine : de l'adsorption sur les nanoparticules aux gels nanocomposites Protein−Nanoparticle Interactions: What Are the Protein−Corona Thickness and Organization? In Situ Analysis of Weakly Bound Proteins Reveals Molecular Basis of Soft Corona Formation." Thesis, université Paris-Saclay, 2021. http://www.theses.fr/2021UPASF011.

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Les gels de protéine nanocomposites sont un sujet encore peu développé dans la littérature malgré de nombreuses applications allant de l’immobilisation d’enzyme aux prothèses en passant par les gels alimentaires. La protéine permet d’assurer la biocompatibilité des gels tandis que l’ajout des nanoparticules a pour but de moduler les propriétés mécaniques des gels. Nous avons donc décidé de nous intéresser aux gels d’hémoglobine réticulée chimiquement et dopés aux nanoparticules. L’hémoglobine (Hb) a été choisie pour sa grande abondance et ses propriétés de fixation du dioxygène. Les gels seront obtenus par réticulation par le glutaraldéhyde (GTA), un dialdéhyde très réactif. Les gels seront dopés par des nanoparticules de silice (NP) afin de comprendre déjà l’effet sur le gel du dopage par des nanoparticules modèles. La première partie de la thèse portera sur l’adsorption de l’hémoglobine sur les nanoparticules de silice afin de lever les dernières inconnues sur ce phénomène déjà étudié. Il sera mesuré les isothermes d’adsorption ainsi que l’activité de l’hémoglobine adsorbée. Les structures de l’hème, de la globine et de l’assemblage Hb/NP seront étudiées avec détails. Par la suite, les études se porteront sur les gels sans et avec nanoparticules afin d’élucider les effets de la gélification et du dopage respectivement. On déterminera les concentrations en Hb, GTA et NP permettant d’obtenir un gel. Puis, comme pour les assemblages Hb/NP, nous nous intéresserons à l’activité et à la structure de Hb (hème et globine). La structuration du gel sera de plus étudiée. Des études sur les propriétés élastiques des gels seront aussi menées et nous finirons sur la dynamique de la protéine gélifiée. Quand il sera possible, l’effet des concentrations des différents composants sera déterminé. Pour toutes ces études, il a été utilisé un vaste panel de techniques de caractérisation classique des protéines ou des gels. Beaucoup d’expériences ont été effectuées sur grands instruments (diffusion de rayonnement, spectroscopie d’adsorption X, dichroïsme circulaire). Des techniques plus accessibles comme la résonance paramagnétique électronique, la rhéologie ou la microscopie électronique ont aussi été employées. Les aspects les plus novateurs de cette thèse ont été l’effet de l’adsorption sur l’hème et la compréhension de la structure de la protéine gélifiée, deux aspects qui n’avaient pas été traités
Nanocomposite protein gels are still an underdeveloped subject in the literature despite many applications ranging from enzyme immobilization to prostheses to food gels. The protein ensures the gel biocompatibility while the addition of the nanoparticles will modulate the gel mechanical properties. We decided to focus on chemically cross-linked hemoglobin gels doped with nanoparticles. Hemoglobin (Hb) was chosen for its high abundance and its oxygen binding properties. The gels will be obtained by crosslinking with glutaraldehyde (GTA), a very reactive dialdehyde. The gels will be doped with silica nanoparticles (NP) in order to understand the effect of doping with model nanoparticles on the gel. The first part of the work will focus on the hemoglobin adsorption on silica nanoparticles in order to resolve the remaining unknowns on this phenomenon, which has already been studied. The adsorption isotherms as well as the activity of the adsorbed hemoglobin will be measured. The structures of the heme, globin and the Hb/NP assembly will be studied in details. Subsequently, works will focus on gels without and with nanoparticles in order to respectively elucidate the effects of gelation and doping. We will determine the concentrations of Hb, GTA and NP to obtain a gel. Then, as with the Hb/NP assemblies, we will look at the activity and structure of Hb (heme and globin).The structuring of the gel will also be studied. Works on the gel elastic properties will also be carried out and we will finish on the dynamics of the gelled protein. When possible, the concentration effect for the different components will be determined. For all these studies, a large panel of conventional technics to characterize proteins or gels was used. Many experiments have been performed in synchrotrons and neutron research centers (radiation scattering, X-ray absorption spectroscopy, circular dichroism). Electronic paramagnetic resonance, rheology or electron microscopy, which are more accessible technics have also been employed. The most innovative aspects of this work were the effect of adsorption on heme and the understanding of the gelled protein structure, two aspects that had not been addressed until now
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Books on the topic "Protein nanoparticle"

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Rahman, Masoud, Sophie Laurent, Nancy Tawil, L'Hocine Yahia, and Morteza Mahmoudi. Protein-Nanoparticle Interactions. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-37555-2.

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Kumar, Ashutosh, and Alok Dhawan, eds. Nanoparticle–Protein Corona. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308.

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Rahman, Masoud. Protein-Nanoparticle Interactions: The Bio-Nano Interface. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013.

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Wang, Jianpeng. Study of the Peptide-Peptide and Peptide-Protein Interactions and Their Applications in Cell Imaging and Nanoparticle Surface Modification. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-53399-4.

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Podzimek, Stepan. Light scattering, size exclusion chromatography, and asymmetric flow field flow fractionation: Powerful tools for the characterization of polymers, proteins and nanoparticles. Hoboken, N.J: Wiley, 2011.

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Min, Zhang, Yin Bin-Cheng, and SpringerLink (Online service), eds. Nano-Bio Probe Design and Its Application for Biochemical Analysis. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012.

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Dhawan, Alok, and Ashutosh Kumar. Nanoparticle-Protein Corona: Biophysics to Biology. Royal Society of Chemistry, The, 2019.

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Laurent, Sophie, L'Hocine Yahia, Masoud Rahman, Morteza Mahmoudi, and Nancy Tawil. Protein-Nanoparticle Interactions: The Bio-Nano Interface. Springer, 2015.

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Laurent, Sophie, Masoud Rahman, and Nancy Tawil. Protein-Nanoparticle Interactions: The Bio-Nano Interface. Springer, 2013.

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Wang, Jianpeng. Study of the Peptide-Peptide and Peptide-Protein Interactions and Their Applications in Cell Imaging and Nanoparticle Surface Modification. Springer, 2016.

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Book chapters on the topic "Protein nanoparticle"

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Shah, Juhi, and Sanjay Singh. "CHAPTER 1. Nanoparticle–Protein Corona Complex: Composition, Kinetics, Physico–Chemical Characterization, and Impact on Biomedical Applications." In Nanoparticle–Protein Corona, 1–30. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00001.

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Forest, V. "CHAPTER 2. Biological Significance of the Nanoparticles Protein Corona." In Nanoparticle–Protein Corona, 31–60. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00031.

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Patel, Pal, and Ashutosh Kumar. "CHAPTER 3. Factors Affecting a Nanoparticle's Protein Corona Formation." In Nanoparticle–Protein Corona, 61–79. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00061.

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Panchal, Divya, Ruchit Patel, Manthan Siddheshwari, Efftesum Rahaman, Vaishwik Patel, and Ajay S. Karakoti. "CHAPTER 4. NP–Protein Corona Interaction: Characterization Methods and Analysis." In Nanoparticle–Protein Corona, 80–131. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00080.

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Raijiwala, Paula, Alok Pandya, and Ritesh K. Shukla. "CHAPTER 5. An Analytical Approach to Investigate Nanoparticle–Protein Corona Complexes." In Nanoparticle–Protein Corona, 132–62. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00132.

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Dubey, Kavita, Onila Lugun, and Alok Kumar Pandey. "CHAPTER 6. Impact of Nanoparticle–Protein Interactions on Biological Assays." In Nanoparticle–Protein Corona, 163–90. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00163.

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Baweja, Lokesh. "CHAPTER 7. Computer Simulations for Understanding Nanoparticle-biomolecule Corona Formation." In Nanoparticle–Protein Corona, 191–203. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00191.

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Globisch, Christoph, Marc Isele, Christine Peter, and Alok Jain. "CHAPTER 8. In Silico Approaches to Design and Characterize Peptide-based Nanostructures." In Nanoparticle–Protein Corona, 204–26. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00204.

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Singh, Priti, and Sunil Kumar Singh. "CHAPTER 9. Nanomaterial–Blood Interactions: A Biomedical Perspective." In Nanoparticle–Protein Corona, 227–64. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00227.

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Alex, Sruthi Ann, Debolina Chakraborty, N. Chandrasekaran, and Amitava Mukherjee. "CHAPTER 10. The Protein Corona: Applications and Challenges." In Nanoparticle–Protein Corona, 265–86. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788016308-00265.

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Conference papers on the topic "Protein nanoparticle"

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Movahedi, Marziyeh, Fatemeh Zare-Mirakabad, Ali Ramazani, Nagarjun Konduru, and Seyed Shahriar Arab. "Computational Analysis of Nanoparticle Features on Protein Corona Composition in Biological Nanoparticle-Protein Interactions." In 2019 5th Conference on Knowledge Based Engineering and Innovation (KBEI). IEEE, 2019. http://dx.doi.org/10.1109/kbei.2019.8735000.

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Kumar, Sugam, I. Yadav, V. K. Aswal, and J. Kohlbrecher. "Modifications in nanoparticle-protein interactions by varying the protein conformation." In DAE SOLID STATE PHYSICS SYMPOSIUM 2016. Author(s), 2017. http://dx.doi.org/10.1063/1.4980309.

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Mehan, Sumit, V. K. Aswal, and J. Kohlbrecher. "Probing nanoparticle effect in protein-surfactant complexes." In NANOFORUM 2014. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4917667.

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Yue Zhuo, Limei Tian, Weili Chen, Hojeong Yu, Srikanth Singamaneni, and Brian T. Cunningham. "Protein-protein binding detection with nanoparticle photonic crystal enhanced microscopy (NP-PCEM)." In 2014 36th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2014. http://dx.doi.org/10.1109/embc.2014.6944023.

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Pons, Thomas. "Nanoparticle zwitterionic coatings: evading protein corona in serum and cytoplasm (Conference Presentation)." In Colloidal Nanoparticles for Biomedical Applications XV, edited by Marek Osiński and Antonios G. Kanaras. SPIE, 2020. http://dx.doi.org/10.1117/12.2545549.

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Frau, Eleonora, and Silvia Schintke. "Towards Standards for Light Scattering Studies of Proteins Stability and Nanoparticle-Protein Interactions." In 2020 22nd International Conference on Transparent Optical Networks (ICTON). IEEE, 2020. http://dx.doi.org/10.1109/icton51198.2020.9203371.

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Kumar, Sugam, V. K. Aswal, and P. Callow. "Tuning structure of oppositely charged nanoparticle and protein complexes." In SOLID STATE PHYSICS: Proceedings of the 58th DAE Solid State Physics Symposium 2013. AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4872529.

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Yang, Xi, Yanqiong Wang, Yiling Liu, Wanjing Zhao, Yun-Jiang Rao, and Yuan Gong. "Nanoparticle-based fiber optofluidic laser for label-free protein detection." In 2021 IEEE International Instrumentation and Measurement Technology Conference (I2MTC). IEEE, 2021. http://dx.doi.org/10.1109/i2mtc50364.2021.9459803.

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Joshi, Deepti, and R. K. Soni. "Laser Induced Gold Nanoparticle Egg-White Protein Conjugation and Thermal Denaturation." In International Conference on Fibre Optics and Photonics. Washington, D.C.: OSA, 2012. http://dx.doi.org/10.1364/photonics.2012.mpo.3.

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Zyubin, Andrey, Vladimir Rafalskiy, Karina I. Matveeva, Ekaterina Moiseeva, Alina Tsapkova, Elizaveta Demishkevich, Ilia G. Samusev, and Valery Bryukhanov. "Photophysical properties of nanoparticle-dye-protein complexes for fluorescent labeling purposes." In Plasmonics V, edited by Zheyu Fang and Takuo Tanaka. SPIE, 2020. http://dx.doi.org/10.1117/12.2575386.

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Reports on the topic "Protein nanoparticle"

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Wang, Lijun. Studies of the structure and function of Mms6, a bacterial protein that promotes the formation of magnetic nanoparticles. Office of Scientific and Technical Information (OSTI), January 2011. http://dx.doi.org/10.2172/1029600.

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