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Статті в журналах з теми "Protein/peptides drug delivery"

1

Dahiya, Sunita, and Rajiv Dahiya. "BIOAVAILABILITY ENHANCEMENT AND LIPID NANOCARRIER BASED DELIVERY OF PEPTIDES AND PROTEINS." Bulletin of Pharmaceutical Research 10, no. 1-3 (2020): 1–10. http://dx.doi.org/10.21276/bpr.2020.10.3.

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Peptides and proteins are vital biomacromolecules that perform several bodily functions in various physiological and biological processes. Being biocompatible and biodegradable, these macromolecules are considered promising platforms for delivery of drugs and genes. However, peptides and proteins suffer from major limitations including enzymatic degradation, short circulation half-lives, and poor membrane permeability that leads to poor bioavailability, challenging their effective delivery. This article briefly discusses the inherent challenges in peptide and protein delivery along with strategies for bioavailability enhancement and lipid nanocarriers as prospective systems for peptide and protein drug delivery.
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Lakshmi, P. k., D. Prasanthi, and B. Veeresh. "NON INVASIVE DELIVERY OF PROTEIN AND PEPTIDE DRUGS: A REVIEW." Asian Journal of Pharmaceutical and Clinical Research 10, no. 8 (August 1, 2017): 25. http://dx.doi.org/10.22159/ajpcr.2017.v10i8.18274.

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Till recent, injections remained the most common route for administration of protein and peptide drugs because of their poor bioavailability in the other routes. Because it is generally recognized that injection based delivery is a major impediment to the commercial success of therapeutic proteins and peptides, research in both academia and industry continues to focus on ways to overcome this problem. Possible non-parenteral administration routes for delivery of peptide and protein drugs include oral, nasal, ocular, transdermal, rectal, colonic, and vaginal route. The large surface area associated with most of these routes makes them attractive targets for drug delivery. While non-invasive administration by these routes is considered a more logical and achievable option for local treatment regimens, systemic delivery of proteins and peptides is significantly more challenging. In spite of effort made on the development of drugs for these routes, most of the successes fail to address how the technology will be transformed to a commercial product. The only notable exceptions have been the successful commercialization of nasal formulations for systemic delivery of a limited number of therapeutic peptides, and recent regulatory approvals of both pulmonary and buccal delivery systems for systemic delivery of insulin and an oral formulation of a small peptide analog, cyclosporine, have been commercialized. The present review aims to discuss the potential non-invasive routes of protein and peptide drug delivery. The factors which will affect drug transport and the bioavailability of proteins administered through these routes is also emphasized
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3

Berillo, Dmitriy, Adilkhan Yeskendir, Zharylkasyn Zharkinbekov, Kamila Raziyeva, and Arman Saparov. "Peptide-Based Drug Delivery Systems." Medicina 57, no. 11 (November 5, 2021): 1209. http://dx.doi.org/10.3390/medicina57111209.

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Peptide-based drug delivery systems have many advantages when compared to synthetic systems in that they have better biocompatibility, biochemical and biophysical properties, lack of toxicity, controlled molecular weight via solid phase synthesis and purification. Lysosomes, solid lipid nanoparticles, dendrimers, polymeric micelles can be applied by intravenous administration, however they are of artificial nature and thus may induce side effects and possess lack of ability to penetrate the blood-brain barrier. An analysis of nontoxic drug delivery systems and an establishment of prospective trends in the development of drug delivery systems was needed. This review paper summarizes data, mainly from the past 5 years, devoted to the use of peptide-based carriers for delivery of various toxic drugs, mostly anticancer or drugs with limiting bioavailability. Peptide-based drug delivery platforms are utilized as peptide–drug conjugates, injectable biodegradable particles and depots for delivering small molecule pharmaceutical substances (500 Da) and therapeutic proteins. Controlled drug delivery systems that can effectively deliver anticancer and peptide-based drugs leading to accelerated recovery without significant side effects are discussed. Moreover, cell penetrating peptides and their molecular mechanisms as targeting peptides, as well as stimuli responsive (enzyme-responsive and pH-responsive) peptides and peptide-based self-assembly scaffolds are also reviewed.
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4

Salmaso, Stefano, Sara Bersani, Alessandra Semenzato, and Paolo Caliceti. "Nanotechnologies in Protein Delivery." Journal of Nanoscience and Nanotechnology 6, no. 9 (September 1, 2006): 2736–53. http://dx.doi.org/10.1166/jnn.2006.456.

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Анотація:
The growth rate for biotech drugs, namely proteins, peptides, and oligonucleotides, is dictated by the parallel progresses in biotechnology and nanotechnology. Actually, biotechnology techniques have expanded enormously the arsenal of therapeutically useful peptides and proteins making these products of primary interest for future pharmaceutical market. Nevertheless, the exploitation of protein and peptide drugs is strictly related to the development of innovative delivery systems which should provide for controlled, prolonged, or targeted delivery, improved stability during storage and delivery, reduced adverse effects, increased bioavailability, improved patient compliance and allow for administration through the desired route and cope with cost-containment therapeutic protocols. Colloidal formulations ideally possess the physicochemical and biopharmaceutical requisites for protein delivery. Pharmaceutical nanotechnology is a tool of techniques applied to design, develop and produce these systems. It involves the investigation of innovative materials and production procedures for preparation of a variety of nanosized dosage forms, which range from solid nanoparticles to soluble bioconjugates. The research and development of innovative tailor made protein delivery systems, which must be designed according to the drug candidate pharmacological and physicochemical properties, is one of the primary aim of modern pharmaceutical technology. Therefore, as an unmet need exists for technologies that combine innovative drug delivery solutions, a close un-prejudicial interaction between academic and industrial researchers as well as business thought leaders is required.
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Er, Simge, Ushna Laraib, Rabia Arshad, Saman Sargazi, Abbas Rahdar, Sadanand Pandey, Vijay Kumar Thakur, and Ana M. Díez-Pascual. "Amino Acids, Peptides, and Proteins: Implications for Nanotechnological Applications in Biosensing and Drug/Gene Delivery." Nanomaterials 11, no. 11 (November 8, 2021): 3002. http://dx.doi.org/10.3390/nano11113002.

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Анотація:
Over various scientific fields in biochemistry, amino acids have been highlighted in research works. Protein, peptide- and amino acid-based drug delivery systems have proficiently transformed nanotechnology via immense flexibility in their features for attaching various drug molecules and biodegradable polymers. In this regard, novel nanostructures including carbon nanotubes, electrospun carbon nanofibers, gold nanoislands, and metal-based nanoparticles have been introduced as nanosensors for accurate detection of these organic compounds. These nanostructures can bind the biological receptor to the sensor surface and increase the surface area of the working electrode, significantly enhancing the biosensor performance. Interestingly, protein-based nanocarriers have also emerged as useful drug and gene delivery platforms. This is important since, despite recent advancements, there are still biological barriers and other obstacles limiting gene and drug delivery efficacy. Currently available strategies for gene therapy are not cost-effective, and they do not deliver the genetic cargo effectively to target sites. With rapid advancements in nanotechnology, novel gene delivery systems are introduced as nonviral vectors such as protein, peptide, and amino acid-based nanostructures. These nano-based delivery platforms can be tailored into functional transformation using proteins and peptides ligands based nanocarriers, usually overexpressed in the specified diseases. The purpose of this review is to shed light on traditional and nanotechnology-based methods to detect amino acids, peptides, and proteins. Furthermore, new insights into the potential of amino protein-based nanoassemblies for targeted drug delivery or gene transfer are presented.
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6

Kim, WonJu, and Je-Min Choi. "Development of a novel transcutaneous delivery peptide and its application in skin inflammation (HYP7P.273)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 191.21. http://dx.doi.org/10.4049/jimmunol.194.supp.191.21.

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Abstract Transcutaneous delivery of therapeutic drugs has many advantages over the systemic administration for inflammatory skin diseases such as atopic dermatitis or psoriasis. However, the greatest challenge for transcutaneous delivery is methodology due to the tight junction of skin tissue. Here, we screened and identified transdermal delivery peptide (TDP) from human proteins which would be non-invasive and simple method to deliver various cargos such as chemicals, peptides, proteins, etc. TDP-EGFP recombinant protein was purified and exhibited significantly higher intracellular transduction efficacy compared with TAT-EGFP in Jurkat, HaCaT, NIH3T3 cell lines and also in primary cells including splenocytes and keratinocytes. TDP-TAMRA peptides were successfully delivered into the epidermis and dermis of the mouse ear and back skin. We also used TDP-VIVIT peptide to inhibit T cell activation and contact dermatitis in vivo. TDP-VIVIT significantly inhibited IL-2 secretion with reduction of CD69 and CD44 expression level of activated CD4 and CD8 T cells. Our results suggest TDP-VIVIT peptide could be a potential transdermal applicable therapeutic drug for inflammatory skin diseases.
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7

Mukherjee, Biswajit, Swapna Karmakar, Chowdhury Hossain, and Sanchari Bhattacharya. "Peptides, Proteins and Peptide/Protein-Polymer Conjugates as Drug Delivery System." Protein & Peptide Letters 21, no. 11 (August 4, 2014): 1121–28. http://dx.doi.org/10.2174/0929866521666140804160907.

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8

Kumar, Vinod, Sumeet Patiyal, Anjali Dhall, Neelam Sharma, and Gajendra Pal Singh Raghava. "B3Pred: A Random-Forest-Based Method for Predicting and Designing Blood–Brain Barrier Penetrating Peptides." Pharmaceutics 13, no. 8 (August 11, 2021): 1237. http://dx.doi.org/10.3390/pharmaceutics13081237.

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The blood–brain barrier is a major obstacle in treating brain-related disorders, as it does not allow the delivery of drugs into the brain. We developed a method for predicting blood–brain barrier penetrating peptides to facilitate drug delivery into the brain. These blood–brain barrier penetrating peptides (B3PPs) can act as therapeutics, as well as drug delivery agents. We trained, tested, and evaluated our models on blood–brain barrier peptides obtained from the B3Pdb database. First, we computed a wide range of peptide features. Then, we selected relevant peptide features. Finally, we developed numerous machine-learning-based models for predicting blood–brain barrier peptides using the selected features. The random-forest-based model performed the best with respect to the top 80 selected features and achieved a maximal 85.08% accuracy with an AUROC of 0.93. We also developed a webserver, B3pred, that implements our best models. It has three major modules that allow users to predict/design B3PPs and scan B3PPs in a protein sequence.
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9

Rubin, Samuel J. S., and Nir Qvit. "Engineering “Antimicrobial Peptides” and Other Peptides to Modulate Protein-Protein Interactions in Cancer." Current Topics in Medicinal Chemistry 20, no. 32 (December 3, 2020): 2970–83. http://dx.doi.org/10.2174/1568026620666201021141401.

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Antimicrobial peptides (AMPs) are a class of peptides found across a wide array of organisms that play key roles in host defense. AMPs induce selective death in target cells and orchestrate specific or nonspecific immune responses. Many AMPs exhibit native anticancer activity in addition to antibacterial activity, and others have been engineered as antineoplastic agents. We discuss the use of AMPs in the detection and treatment of cancer as well as mechanisms of AMP-induced cell death. We present key examples of cathelicidins and transferrins, which are major AMP families. Further, we discuss the critical roles of protein-protein interactions (PPIs) in cancer and how AMPs are well-suited to target PPIs based on their unique drug-like properties not exhibited by small molecules or antibodies. While peptides, including AMPs, can have limited stability and bioavailability, these issues can be overcome by peptide backbone modification or cyclization (e.g., stapling) and by the use of delivery systems such as cellpenetrating peptides (CPPs), respectively. We discuss approaches for optimizing drug properties of peptide and peptidomimetic leads (modified peptides), providing examples of promising techniques that may be applied to AMPs. These molecules represent an exciting resource as anticancer agents with unique therapeutic advantages that can target challenging mechanisms involving PPIs. Indeed, AMPs are suitable drug leads for further development of cancer therapeutics, and many studies to this end are underway.
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10

Yu, Xiaoxuan, Zihui Weng, Ziyang Zhao, Jiayun Xu, Zhenhui Qi, and Junqiu Liu. "Assembly of Protein Cages for Drug Delivery." Pharmaceutics 14, no. 12 (November 26, 2022): 2609. http://dx.doi.org/10.3390/pharmaceutics14122609.

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Nanoparticles (NPs) have been widely used as target delivery vehicles for therapeutic goods; however, compared with inorganic and organic nanomaterials, protein nanomaterials have better biocompatibility and can self-assemble into highly ordered cage-like structures, which are more favorable for applications in targeted drug delivery. In this review, we concentrate on the typical protein cage nanoparticles drugs encapsulation processes, such as drug fusion expression, diffusion, electrostatic contact, covalent binding, and protein cage disassembly/recombination. The usage of protein cage nanoparticles in biomedicine is also briefly discussed. These materials can be utilized to transport small molecules, peptides, siRNA, and other medications for anti-tumor, contrast, etc.
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Дисертації з теми "Protein/peptides drug delivery"

1

Vellore, Janarthanan Mohanraj. "Formulation of chitosan-based nanoparticles for delivery of proteins and peptides." Thesis, Curtin University, 2003. http://hdl.handle.net/20.500.11937/1224.

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Delivery of complex molecules such as peptides, proteins, oligonucleotides and plasmids is an intensively studied subject, which has attracted considerable medical and pharmaceutical interest. Encapsulation of these molecules with biodegradable polymers represents one way of overcoming various problems associated with the conventional delivery of macromolecules, for example instability and short biological half-life. The use of carriers made of hydrophilic polysaccharides such as chitosan, has been pursued as a promising alternative for improving the transport of biologically active macromolecules across biological surfaces. The development of nanoparticles as a delivery system also has major advantages of achieving possible drug protection, controlled release and drug targeting by either a passive or an active means. The aim of this study was to develop a simple and effective method to formulate biodegradable nanoparticles for the delivery of a model protein-bovine serum albumin (BSA) and an angiogenesis inhibitor, arginine-rich hexapeptide (ARE peptide). Major factors which determine nanoparticle formation and loading of the protein and the peptide as well as the underlying mechanisms controlling their incorporation and release characteristics were investigated. The preparation technique, based on the complex coacervation process, is extremely mild and involves the mixture of two aqueous solutions (chitosan and dextran sulfate) at room temperature. The formation of nanoparticles is dependent on the concentrations of chitosan (CS) and dextran sulfate (DS); particles with size, of 257 to 494nm can be obtained with 0.1%w/v solutions of CS and DS. Zeta potential of nanoparicles can be modulated conveniently from -34.3mV to +52.7mV by varying the composition of the two ionic polymers.Both bovine BSA and the ARH peptide were successfully incorporated into CS-based nanoparticles, mainly via an electrostatic interaction, with entrapment efficiency up to 100% and 75.9% for the protein and peptide respectively. Incorporation of both the protein and peptide into nanoparticles resulted in an increase in size suggesting their close association with the nanoparticle matrix material. The difference in sign and magnitude of zeta potential of empty and macromolecules-loaded nanoparticles supports the hypothesis that protein and peptide association with nanoparticles can be modulated by their ionic interaction with the oppositely charged ionic polymer (DS) in the nanoparticles. The release of BSA from the nanoparticles was very slow in water compared to that in l0mM phosphate buffer pH 7.4; whereas, ARH peptide showed extremely low level of release in water at the low ratio of DS but at the high ratio of DS, its release was in biphasic fashion, with an initial burst effect followed by an almost constant but very slow release up to 7 days in both water and 1 OmM phosphate buffer (pH 7.4). It was found that, unlike ARH peptide, the percentage of BSA released was relatively slower for the nanoparticles with a high ratio of DS. It is speculated that this difference in the release behaviour of BSA and ARH peptide, could be due to the effect of molecular size of the compounds and their interaction with the polymer matrix of the nanoparticle. The results of this study suggest that these novel CS/DS nanoparticulate system, prepared by a very mild ionic crosslinking technique, have potential to be a suitable carrier for the entrapment and controlled release of peptides and proteins.
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2

Abdulrazzaq, Fadi. "Aquasomes as a drug delivery system for proteins and peptides." Thesis, Aston University, 2016. http://publications.aston.ac.uk/30080/.

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Aquasomes are nanocarrier systems consist of three distinctive layers; an inner core, a polyhydroxy carbohydrate layer and an outer layer of an API (Kossovsky et al., 1991). Aquasomes have a unique structure and ability to carry active molecules through a non-covalent bounding and provide superior stability, especially for proteins and peptides (Masatoshi and Yongning, 1998; Kim and Kim, 2002; Khopade et al., 2002). Different core and coating materials were used to prepare aquasomes under different conditions to investigate the relationship between preparation conditions and loading efficiency. In terms of loading efficiency, hydroxyapatite aquasomes, with either lactose or trehalose as a coating material, had the highest BSA loading (40%-60%) when compared to DSPA aquasomes. While DCPA aquasomes, with either lactose or trehalose as a coating material, had the lowest BSA loading (8%-16%). To investigate the interaction of the three layers of aquasomes, Surface analysis, docking and MD simulations were performed. Surface analysis performed by Discovery Studio showed that HA and trehalose interact by hydrogen bonding with the later acting as a hydrogen acceptor, while BSA displayed almost complete SAS and that there are numerous targets for trehalose attachments (no specific active site). MD simulations of BSA performed by AMBER 12 showed a stable MD simulation of BSA for 5 ns. Total energy analysis of BSA on the two conditions performed (300K and 280K) support the experimental data of lower BSA loadings of aquasomes prepared at 400C compared to those manufactured at 250C (p < 0.05). This could be related to that BSA might have either started to denature/unfold or breaking up which eventually resulted in low BSA loadings obtained experimentally. The high loading efficiency highlights aquasomes as a promising carrier for the delivery of proteins and peptides. Following formulation Optimisation, two routes of delivery were investigated, pulmonary and oral routes. For pulmonary delivery of aquasomes, BSA-loaded aquasomes were successfully formulated as pMDI and DPI formulations. Both pMDI and DPI formulations were investigated to identify lung distribution of BSA-loaded aquasomes using NGI. In vitro release studies on the selected size fractions from NGI show a sustained release of BSA over a period of 6 hr. In order to complement the in vitro release data, cell culture studies were performed to demonstrate the controlled release effect of aquasomes with BEAS-2B cell lines. The release of salbutamol sulphate (model drug) from aquasomes post 2 hr started to slow gradually until it reached its highest difference at 6 hr (p<0.05) when compared to the control. For oral delivery of aquasomes, BSA-loaded aquasome tablets were successfully formulated with MCC as multifunctional excipient and talc as a lubricant. Various powder blends of varying aquasomes amounts (25, 37.5, 50, 62.5 and 75%) were prepared and compressed at increasing compression forces (0.5, 1, 2 and 3 tons). It was noticed that under high compression forces of 2 and 3 tons, BSA spreads out of BSA-loaded aquasomes as was presented with confocal microscopy images. Tablets compressed under 1 ton of compression force was therefore chosen for coating as it showed desirable tablet characteristics (hardness, disintegration etc.). Acrylic based coating was used to spray coat the tablets. The coated tablets were found to disintegrate in pH >5.5 and steadily release for 6 hr. Cell culture studies were conducted to demonstrate the controlled release effect of aquasomes using Caco-2 cell lines. The release of metronidazole (model drug) from aquasomes post 2 hr started to slow gradually until it reached its highest difference at 6 hr (p<0.05) when compared to the control.
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3

Soane, Robert J. "Bioadhesive polymers as intranasal drug delivery systems for peptide and protein drugs." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298078.

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4

Vellore, Janarthanan Mohanraj. "Formulation of chitosan-based nanoparticles for delivery of proteins and peptides." Curtin University of Technology, School of Pharmacy, 2003. http://espace.library.curtin.edu.au:80/R/?func=dbin-jump-full&object_id=14517.

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Анотація:
Delivery of complex molecules such as peptides, proteins, oligonucleotides and plasmids is an intensively studied subject, which has attracted considerable medical and pharmaceutical interest. Encapsulation of these molecules with biodegradable polymers represents one way of overcoming various problems associated with the conventional delivery of macromolecules, for example instability and short biological half-life. The use of carriers made of hydrophilic polysaccharides such as chitosan, has been pursued as a promising alternative for improving the transport of biologically active macromolecules across biological surfaces. The development of nanoparticles as a delivery system also has major advantages of achieving possible drug protection, controlled release and drug targeting by either a passive or an active means. The aim of this study was to develop a simple and effective method to formulate biodegradable nanoparticles for the delivery of a model protein-bovine serum albumin (BSA) and an angiogenesis inhibitor, arginine-rich hexapeptide (ARE peptide). Major factors which determine nanoparticle formation and loading of the protein and the peptide as well as the underlying mechanisms controlling their incorporation and release characteristics were investigated. The preparation technique, based on the complex coacervation process, is extremely mild and involves the mixture of two aqueous solutions (chitosan and dextran sulfate) at room temperature. The formation of nanoparticles is dependent on the concentrations of chitosan (CS) and dextran sulfate (DS); particles with size, of 257 to 494nm can be obtained with 0.1%w/v solutions of CS and DS. Zeta potential of nanoparicles can be modulated conveniently from -34.3mV to +52.7mV by varying the composition of the two ionic polymers.
Both bovine BSA and the ARH peptide were successfully incorporated into CS-based nanoparticles, mainly via an electrostatic interaction, with entrapment efficiency up to 100% and 75.9% for the protein and peptide respectively. Incorporation of both the protein and peptide into nanoparticles resulted in an increase in size suggesting their close association with the nanoparticle matrix material. The difference in sign and magnitude of zeta potential of empty and macromolecules-loaded nanoparticles supports the hypothesis that protein and peptide association with nanoparticles can be modulated by their ionic interaction with the oppositely charged ionic polymer (DS) in the nanoparticles. The release of BSA from the nanoparticles was very slow in water compared to that in l0mM phosphate buffer pH 7.4; whereas, ARH peptide showed extremely low level of release in water at the low ratio of DS but at the high ratio of DS, its release was in biphasic fashion, with an initial burst effect followed by an almost constant but very slow release up to 7 days in both water and 1 OmM phosphate buffer (pH 7.4). It was found that, unlike ARH peptide, the percentage of BSA released was relatively slower for the nanoparticles with a high ratio of DS. It is speculated that this difference in the release behaviour of BSA and ARH peptide, could be due to the effect of molecular size of the compounds and their interaction with the polymer matrix of the nanoparticle. The results of this study suggest that these novel CS/DS nanoparticulate system, prepared by a very mild ionic crosslinking technique, have potential to be a suitable carrier for the entrapment and controlled release of peptides and proteins.
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5

Capriotti, Lisa A. "Surface-induced peptide folding." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 347 p, 2009. http://proquest.umi.com/pqdweb?did=1824967161&sid=6&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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6

Ali, Stuart Alvaro. "Transferrin trojan horses : a novel approach for drug delivery?" Thesis, Brunel University, 1999. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285047.

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7

Lei, Xia. "Study of Zwitterionic Functionalized Materials for Drug Delivery and Protein Therapeutics." University of Akron / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=akron1555511296878391.

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8

Qian, Ziqing. "Developments and Applications of Cyclic Cell Penetrating Peptides." The Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1405340891.

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9

Mozaffari, Saghar. "Amphiphilic Cell-Penetrating Hybrid Cyclic-Linear Peptides as a Drug Delivery System." Chapman University Digital Commons, 2019. https://digitalcommons.chapman.edu/pharmaceutical_sciences_dissertations/2.

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A number of cyclic peptides containing a positively charged ring composed of arginine residues attached to hydrophobic tail made of tryptophan residues through a lysine linker namely [R5K]W5, [R6K]W5, [R5K]W6, [R7K]W5, [R5K]W7, [R6K]W6, and [R7K]W7 were synthesized and evaluated as molecular transporters. The peptides were evaluated for their ability to deliver, fluorescence-labeled cell-impermeable negatively charged phosphopeptide (F′-GpYEEI), and fluorescent labeled anti-HIV drugs (F′-FTC and F′-d4T). The results indicated that the presence of positively charged arginine residues on the ring and hydrophobic tryptophan residues in a sequential linear outside the ring was an optimal approach to improve the intracellular uptake of cargo molecules through non-covalent interactions. Some of these peptides were also evaluated for their efficiency for intracellular delivery of siRNA to triple-negative breast cancer cell lines in the presence and absence of 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE). [R6K]W6 and [R5K]W5 were found to be very efficient in the delivery of siRNA. Furthermore, co-formulation of peptides with lipid DOPE significantly enhanced the efficiency of siRNA delivery compared to peptide alone. Silencing of kinesin spindle protein (KSP) and Janus kinase 2 (JAK2) was evaluated in MDA-MB-231 cells in the presence of the peptides. The addition of DOPE significantly enhanced the silencing efficiency for all selected peptides. A chemotherapeutic drug, doxorubicin (Dox) was covalently conjugated to the cyclic peptide [R5K]W7A and linear peptide R5KW7A, and the biological activity was evaluated in cell-based assays. Comparative antiproliferative assays between covalently conjugated peptide-Dox and the corresponding noncovalent physical mixtures of the peptides and Dox were performed. The conjugation of Dox with cyclic [R5K]W7A-Dox exhibited similar antiproliferative activity compared to Dox alone after 72 h incubation time in all cancer cell lines, such as leukemia, ovarian and gastric cancer cells. However, [R5K]W7A-Dox significantly reduced the cell cytotoxicity in normal cell lines such as normal heart muscle and normal kidney cells after 72 h when compared with Dox alone. These results revealed that this cyclic peptide prodrug can be used as a potential candidate for the treatment of cancer cells with reduced side effects against normal cells in the body.
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10

Nadal, Bufi Ferran. "Peptide-based drugs to inhibit LDH5, a potential target for cancer therapy." Thesis, Queensland University of Technology, 2022. https://eprints.qut.edu.au/232526/1/Ferran_Nadal%20Bufi_Thesis.pdf.

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This thesis investigates novel strategies to target lactate dehydrogenase 5 (LDH5), a protein involved in cancer. After decades of research without success, this thesis reports the development of the first molecules able to inhibit the activity of LDH5 with an alternative mechanism of action: disrupting its structure. To do that, an emerging class of drugs called peptides are explored. The lead peptide of this work successfully kills breast cancer cells via LDH5 inhibition. The validation of this strategy is relevant because it can be applied to many other cancer targets that have been traditionally considered “undruggable”.
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Книги з теми "Protein/peptides drug delivery"

1

Peptide and protein delivery. London: Academic Press, 2011.

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2

Banga, Ajay K. Therapeutic peptides and proteins: Formulation, processing, and delivery systems. 2nd ed. Boca Raton, FL: CRC/Taylor & Francis, 2006.

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3

Banga, Ajay K. Therapeutic peptides and proteins: Formulation, processing, and delivery systems. Lancaster, Pa: Technomic Pub., 1995.

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4

1949-, Adjei Akete Lex, and Gupta Pramod K. 1959-, eds. Inhalation delivery of therapeutic peptides and proteins. New York: M. Dekker, 1997.

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5

Lee, Vincent H. L., 1951-, Hashida Mitsuru, and Mizushima Yutaka, eds. Trends and future perspectives in peptide and protein drug delivery. Chur, Switzerland: Harwood Academic, 1995.

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6

Lene, Jorgensen, and Nielsen Hanne Mørck, eds. Delivery technologies for biopharmaceuticals: Peptides, proteins, nucleic acids, and vaccines. Chichester, West Sussex: John Wiley, 2009.

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7

NATO Advanced Research Workshop on Advanced Drug Delivery Systems for Peptides and Proteins (1986 Copenhagen, Denmark). Delivery systems for peptide drugs. New York: Plenum Press, 1986.

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8

Alfred Benzon Symposium (43rd 1997 Royal Danish Academy of Sciences and Letters). Peptide and protein drug delivery: Proceedings of a symposium held at the Royal Danish Academy of Sciences and Letters, August 17-21, 1997 : Alfred Benzon Symposium 43. Edited by Christrup Lona, Frøkjær Sven 1947-, and Krogsgaard-Larsen Povl. Copenhagen: Munksgaard, 1998.

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9

NATO, Advanced Research Workshop on Advanced Drug Delivery Sytems for Peptides and Proteins (1986 Copenhagen Denmark). Delivery systems for peptide drugs. New York: Plenum in cooperation with NATO Scientific Affairs Division, 1986.

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10

1961-, McNally Eugene J., ed. Protein formulation and delivery. New York: M. Dekker, 2000.

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Більше джерел

Частини книг з теми "Protein/peptides drug delivery"

1

Sarisozen, Can, and Vladimir P. Torchilin. "Intracellular Delivery of Proteins and Peptides." In Drug Delivery, 576–622. Hoboken, NJ: John Wiley & Sons, Inc, 2016. http://dx.doi.org/10.1002/9781118833322.ch23.

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2

Soltero, Rick. "Oral Protein and Peptide Drug Delivery." In Drug Delivery, 189–200. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471475734.ch10.

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3

Lee, Min Jae, Dexi Liu, Guisheng Zhang, and Xiang Gao. "TAT and TAT-Like Peptides for Protein Transduction and Intracellular Drug Delivery." In Cellular Drug Delivery, 95–106. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1007/978-1-59259-745-1_7.

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Wolff, Ron. "Inhaled Proteins and Peptides." In Advances in Pulmonary Drug Delivery, 1–22. Taylor & Francis Group, 6000 Broken Sound Parkway NW, Suite 300, Boca Raton, FL 33487-2742: CRC Press, 2016. http://dx.doi.org/10.1201/9781315311975-2.

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Kueltzo, Lisa A., and C. Russell Middaugh. "Polycationic Peptides and Proteins in Drug Delivery: Focus on Nonclassical Transport." In Drug Delivery, 279–304. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471475734.ch13.

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Kwok, Philip Chi Lip, Rania Osama Salama, and Hak-Kim Chan. "Proteins, Peptides, and Controlled-Release Formulations for Inhalation." In Inhalation Drug Delivery, 121–44. Chichester, UK: John Wiley & Sons, Ltd, 2013. http://dx.doi.org/10.1002/9781118397145.ch7.

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Bontempo, John A. "Parenteral Formulation for Peptides, Proteins, and Monoclonal Antibodies Drugs: A Commercial Development Overview." In Drug Delivery, 321–39. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471475734.ch15.

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Büyüktimkin, Barlas, John Stewart, Kayann Tabanor, Paul Kiptoo, and Teruna J. Siahaan. "Protein and Peptide Conjugates for Targeting Therapeutics and Diagnostics to Specific Cells." In Drug Delivery, 475–502. Hoboken, NJ: John Wiley & Sons, Inc, 2016. http://dx.doi.org/10.1002/9781118833322.ch20.

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Shoyele, Sunday A. "Controlling the Release of Proteins/Peptides via the Pulmonary Route." In Drug Delivery Systems, 141–48. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-210-6_6.

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Dey, Surajit, Ashim K. Mitra, and Ramesh Krishnamoorthy. "Ocular Delivery and Therapeutics of Proteins and Peptides." In Ophthalmic Drug Delivery Systems, 493–514. 2nd ed. London: Routledge, 2021. http://dx.doi.org/10.4324/9781003113423-21.

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Тези доповідей конференцій з теми "Protein/peptides drug delivery"

1

Abioye, Raliat, Caleb Acquah, Chibuike Udenigwe, Nico Huttmann, and Pei Chun Queenie Hsu. "Self-assembly and hydrogelation properties of egg white-derived peptides." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/jzku2300.

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Анотація:
Functional foods are gaining traction as a source of peptides possessing hydrogelation properties. Analysis of peptides (n=429) in egg white protein hydrolysates resulted in the identification of six peptides: IFYCPIAIM, NIFYCPIAIM, VLVNAIVFKGL, YCPIAIMSA, MMYQIGLF, and VYSFSLASRL as prominent self-assembly candidates based on prediction of their aggregation-prone segments. The objective of this study was to characterize the hydrogel formed via self-assembly of the peptides. Of the six peptides studied, NIFYCPIAIM and MMYQIGLF showed promising self-assembly and hydrogelation properties. Thioflavin T kinetics indicated that NIFYCPIAIM possesses the strongest self-assembly property, confirmed by dynamic light scattering which indicated the largest average particle diameter was achieved after 24 hours. Rheological characterization indicated that all six peptides possessed viscoelastic pseudoplastic properties and some were able to regain some level of viscosity following the exertion of shear stress. Finally, transmission electron microscopy of the six peptides showed the development of fibrillar structures of varying morphologies after 24 hours. The remarkable difference in self-assembly and hydrogelation properties of NIFYCPIAIM, IFYCPIAIMSA and YCPIAIMSA, which share a common sequence YCPIAIM, indicate the importance of amino acid sequence in the formation and property of peptide hydrogels. Identification of the egg white-derived peptides with hydrogelation properties shows a promising future for the use of functional foods in applications of drug delivery systems and tissue engineering, in the food, pharmaceutical, cosmetics, and biomedical sectors.
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2

Yeo, Leslie Y., and James R. Friend. "Surface Acoustic Waves: A New Paradigm for Driving Ultrafast Biomicrofluidics." In ASME 2009 Second International Conference on Micro/Nanoscale Heat and Mass Transfer. ASMEDC, 2009. http://dx.doi.org/10.1115/mnhmt2009-18517.

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Surface acoustic waves (SAWs), which are 10 MHz order surface waves roughly 10 nm in amplitude propagating on the surface of a piezoelectric substrate, can offer a powerful method for driving fast microfluidic actuation and microparticle or biomolecule manipulation. We demonstrate that sessile drops can be linearly translated on planar substrates or fluid can be pumped through microchannels at typically one to two orders of magnitude faster than that achievable through current microfluidic technologies. Micromixing can be induced in the same microchannel in which fluid is pumped using the SAW simply by changing the SAW frequency to superimpose a chaotic oscillatory flow onto the uniform through flow. Strong inertial microcentrifugation for micromixing and particle concentration or separation can also be induced via symmetry-breaking. At low SAW amplitudes below that at which flow commences, the transverse standing wave that arises across the microchannel afford particle aggregation and hence sorting on nodal lines. Other microfluidic manipulations are also possible with the SAW. For example, capillary waves excited on a sessile drop by the SAW can be exploited for microparticle or nanoparticle collection and sorting. At higher amplitudes, the large substrate accelerations drives rapid destabilization of the drop interface giving rise to inertial liquid jets or atomization to produce 1–10 μm monodispersed aerosol droplets. These have significant implications for microfluidic chip mass spectrometry interfacing or pulmonary drug delivery. The atomization also provides a convenient means for the synthesis of 150–200 nm polymer or protein particles or to encapsulate proteins, peptides and other therapeutic molecules within biodegradable polymeric shells for controlled release drug delivery. The atomization of thin films containing polymer solutions, in addition, gives produces a unique regular, long-range spatial polymer spot patterning effect whose size and spacing are dependent on the SAW frequency, thus offering a simple and powerful method for surface patterning without requiring physical or chemical templating.
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3

Mező, Gabor, Erika Orbán, Ildikó Szabó, Rózsa Hegedüs, Szilvia Bősze, Miguel Tejeda, Dezső Gaál, Bence Kapuvári, and Marilena Manea. "GnRH based drug delivery systems for targeted tumor therapy." In XIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2009. http://dx.doi.org/10.1135/css200911072.

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4

Ditto, Andrew J., Nikki K. Robbishaw, Matthew J. Panzner, Wiley J. Youngs, and Yang H. Yun. "Targeting Ovarian Cancer Cells With Rapidly Biodegradable L-Tyrosine Polyphosphate Nanoparticles Decorated With Folate." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53138.

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Анотація:
Chemotherapy employs toxic chemicals to kill rapidly dividing cells. Examples of FDA approved antineoplastic drugs include cisplatin, doxorubicin, and paclitaxel. Since most of these drugs are nonspecific, they also damage normal tissues as well as the aberrant tumors. As a result, non-specific therapies have multiple side effects, which include myelosuppression, mucositis, alopecia, nephrotoxicity, and genotoxcity. In order to minimize these issues, researchers have begun to conjugate antineoplastic chemicals with targeting moieties or encapsulate drugs into nanoparticles decorated with compounds, peptides, or proteins that recognize specific cellular receptors, which are upregulated by the neoplastic cells. The targeting moieties aid in the accumulation of these drugs within the blood vessels of carcinomas, while keeping concentrations low in the systemic circulation. Thus, targeted delivery systems are able to minimize the unwanted side effects and increase the efficacy of chemotherapies.
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5

You, Xueqiu, James Jungho Pak, and Jong-hyeon Chang. "Rapidly dissolving silk protein microneedles for transdermal drug delivery." In 2010 IEEE 4th International Conference on Nano/Molecular Medicine and Engineering (NANOMED). IEEE, 2010. http://dx.doi.org/10.1109/nanomed.2010.5749822.

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Ratnayake, W. R. A. P. J., J. W. Damunupola, S. Rajapakse, and A. C. A. Jayasundera. "Nanocellulose-Protein Matrices: A Model System for Controlled Drug Delivery." In International Conference on Nano Science and Nano Technology. The International Institute of Knowledge Management (TIIKM), 2018. http://dx.doi.org/10.17501/23861215.2018.5101.

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Hui Ma, Guang. "Particle System for Protein Drug Delivery: Strategy,Preparation and Application." In 5th Asian Particle Technology Symposium. Singapore: Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-2518-1_246.

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donner, jon, Sebastian A. Thompson, Mark P. Kreuzer, Guillaume Baffou, and Romain Quidant. "Mapping intracellular temperature using Green Fluorescent Protein - From in vitro to in vivo." In Optical Molecular Probes, Imaging and Drug Delivery. Washington, D.C.: OSA, 2013. http://dx.doi.org/10.1364/omp.2013.mth1c.2.

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Syrvatka, Vasyl J., Yurij I. Slyvchuk, Ivan I. Rozgoni, Ivan I. Gevkan, and Oksana V. Shtapenko. "Sensitive and Rapid Assay for Determination of Protein Concentration Using Silver Nanoparticles with Hyaluronan." In Optical Molecular Probes, Imaging and Drug Delivery. Washington, D.C.: OSA, 2015. http://dx.doi.org/10.1364/omp.2015.om4d.3.

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Bracci, Luisa, Chiara Falciani, Alessandro Pini, Jlenia Brunetti, Barbara Lelli, Antonella Accardo, Diego Tesauro, and Giancarlo Morelli. "Abstract 2319: Target selective drug delivery through liposomes labeled with tetra-branched neurotensin peptides." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2319.

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