The Experts below are selected from a list of 105672 Experts worldwide ranked by ideXlab platform
Prasad S. Sarangapani - One of the best experts on this subject based on the ideXlab platform.
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Protein Aggregation particle formation characterization rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
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Protein Aggregation, particle formation, characterization & rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
Harvey W. Blanch - One of the best experts on this subject based on the ideXlab platform.
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Protein Aggregation in silico.
Trends in Biotechnology, 2007Co-Authors: Troy Cellmer, Dusan Bratko, John M. Prausnitz, Harvey W. BlanchAbstract:Protein Aggregation is a challenge to the successful manufacture of Protein therapeutics; it can impose severe limitations on purification yields and compromise formulation stability. Advances in computer power, and the wealth of computational studies pertaining to Protein folding, have facilitated the development of molecular simulation as a tool to investigate Protein misfolding and Aggregation. Here, we highlight the successes of Protein Aggregation studies carried out in silico, with a particular emphasis on studies related to biotechnology. To conclude, we discuss future prospects for the field, and identify several biotechnology-related problems that would benefit from molecular simulation.
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Molecular simulation of Protein Aggregation
Biotechnology and bioengineering, 2007Co-Authors: Dusan Bratko, Troy Cellmer, John M. Prausnitz, Harvey W. BlanchAbstract:Computer simulation offers unique possibilities for investigating molecular-level phenomena difficult to probe experimentally. Drawing from a wealth of studies concerning Protein folding, computational studies of Protein Aggregation are emerging. These studies have been successful in capturing aspects of Aggregation known from experiment and are being used to refine experimental methods aimed at abating Aggregation. Here we review molecular-simulation studies of Protein Aggregation conducted in our laboratory. Specific attention is devoted to issues with implications for biotechnology.
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Molecular simulation of Protein Aggregation
Biotechnology and Bioengineering, 2006Co-Authors: Dusan Bratko, Troy Cellmer, John M. Prausnitz, Harvey W. BlanchAbstract:Computer simulation offers unique possibilities for investigating molecular-level phenomena difficult to probe experimentally. Drawing from a wealth of studies concerning Protein folding, computational studies of Protein Aggregation are emerging. These studies have been successful in capturing aspects of Aggregation known from experiment and are being used to refine experimental methods aimed at abating Aggregation. Here we review molecular-simulation studies of Protein Aggregation conducted in our laboratory. Specific attention is devoted to issues with implications for biotechnology. Biotechnol. Bioeng. 2007;96: 1–8. © 2006 Wiley Periodicals, Inc.
Nihar Ranjan Jana - One of the best experts on this subject based on the ideXlab platform.
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Small-Molecule-Functionalized Hyperbranched Polyglycerol Dendrimers for Inhibiting Protein Aggregation.
Biomacromolecules, 2020Co-Authors: Suman Mandal, Prasanta Panja, Koushik Debnath, Nihar Ranjan Jana, Nikhil R. JanaAbstract:Amyloid Protein Aggregation is responsible for a variety of neurodegenerative diseases, and antiamyloidogenic small molecules are identified for inhibiting such Protein Aggregation at extra-/intracellular space. We show that the nanoparticle form of small molecules offers better antiamyloidogenic performance via enhanced bioavailability and multivalent binding with Protein. Here, we report hyperbranched polyglycerol dendrimers terminated with antiamyloidogenic small molecules such as gallate, tyrosine, and trehalose and their potential in inhibiting lysozyme/huntingtin Protein Aggregation under intra-/extracellular space. The synthesized functional dendrimers are ∼5 nm in size having an average molecular weight of ∼2000 Da, and they are highly biocompatible in nature. We found that functional dendrimers are efficient in micromolar doses with respect to molecular forms that are effective at millimolar concentration. It is observed that the trehalose-terminated dendrimer is more effective in inhibiting Protein Aggregation, whereas the gallate-terminated dendrimer is more effective in disintegrating mature Protein fibrils. This approach can be used to design functional dendrimers as potential nanodrugs for the treatment of various neurodegenerative diseases.
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Small-Molecule-Functionalized Hyperbranched Polyglycerol Dendrimers for Inhibiting Protein Aggregation.
Biomacromolecules, 2020Co-Authors: Suman Mandal, Prasanta Panja, Koushik Debnath, Nihar Ranjan JanaAbstract:Amyloid Protein Aggregation is responsible for a variety of neurodegenerative diseases, and antiamyloidogenic small molecules are identified for inhibiting such Protein Aggregation at extra-/intrac...
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Trehalose-Functionalized Gold Nanoparticle for Inhibiting Intracellular Protein Aggregation.
Langmuir, 2017Co-Authors: Suman Mandal, Koushik Debnath, Nihar Ranjan Jana, Nikhil R. JanaAbstract:Trehalose is a well-known antiamyloidogenic molecule that inhibits Protein Aggregation under the intracellular/extracellular condition, and recent work shows that the nanoparticle form of trehalose can further enhance this performance. Here we have designed a trehalose-functionalized Au nanoparticle that can inhibit the Aggregation of a polyglutamine-containing mutant Protein inside the neuronal cell. Designed nanoparticles have a 20–30 nm Au core with about 350 ± 50 trehalose molecules per particle on the surface on average. They enter the cell, inhibit mutant Protein Aggregation, and enhance the cell survival against toxic Protein aggregates. This work extends the application potential of trehalose for the understanding and treatment of different diseases involving Protein Aggregation.
Samiul Amin - One of the best experts on this subject based on the ideXlab platform.
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Protein Aggregation particle formation characterization rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
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Protein Aggregation, particle formation, characterization & rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
Christopher J Roberts - One of the best experts on this subject based on the ideXlab platform.
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Protein Aggregation - Mechanisms, detection, and control.
International Journal of Pharmaceutics, 2018Co-Authors: Wei Wang, Christopher J RobertsAbstract:Protein Aggregation has been recognized as one of the major challenges in the development and commercialization of successful Protein-based drug products because of the inherent and high Aggregation tendency during various manufacturing processes, storage, and administration. Protein aggregates may impact significantly the product quality, safety and/or efficacy. This review is intended to summarize four major aspects of Protein Aggregation - (1) Aggregation mechanisms, (2) Aggregation-influencing factors, (3) detection of Protein aggregates, and (4) control of Protein Aggregation based on recent literature in this area.
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Protein Aggregation particle formation characterization rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
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Protein Aggregation, particle formation, characterization & rheology
Current Opinion in Colloid and Interface Science, 2014Co-Authors: Samiul Amin, Jai A. Pathak, Gregory V Barnett, Christopher J Roberts, Prasad S. SarangapaniAbstract:In this review, we attempt to give a concise overview of recent progress made in mechanistic understanding of Protein Aggregation, particulate formation and Protein solution rheology. Recent advances in analytical techniques and methods for characterizing Protein Aggregation and the formed Protein particles as well as advancements, technique limitations and controversies in the field of Protein solution rheology are discussed. The focus of the review is primarily on biotherapeutics and Proteins/antibodies that are relevant to that area. As per the remit of Current Opinion in Colloid and Interface Science, here we attempt to stimulate interest in areas of debate. While the field is certainly not mature enough that all problems may be considered resolved and accepted by consensus, we wish to highlight some areas of controversy and debate that need further attention from the scientific community.
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Non-Arrhenius Protein Aggregation.
The AAPS Journal, 2013Co-Authors: Wei Wang, Christopher J RobertsAbstract:Protein Aggregation presents one of the key challenges in the development of Protein biotherapeutics. It affects not only product quality but also potentially impacts safety, as Protein aggregates have been shown to be linked with cytotoxicity and patient immunogenicity. Therefore, investigations of Protein Aggregation remain a major focus in pharmaceutical companies and academic institutions. Due to the complexity of the Aggregation process and temperature-dependent conformational stability, temperature-induced Protein Aggregation is often non-Arrhenius over even relatively small temperature windows relevant for product development, and this makes low-temperature extrapolation difficult based simply on accelerated stability studies at high temperatures. This review discusses the non-Arrhenius nature of the temperature dependence of Protein Aggregation, explores possible causes, and considers inherent hurdles for accurately extrapolating Aggregation rates from conventional industrial approaches for selecting accelerated conditions and from conventional or more advanced methods of analyzing the resulting rate data.
