Investigating molecular and phase stability of protein solutions by a coarse-grained modeling strategy
Investigating molecular and phase stability of protein solutions by a coarse-grained modeling strategy
Engineering Village 2
2006 Elsevier Inc.
Accession number: 06159809183
Title: Investigating molecular and phase stability of protein solutions by a coarse-grained modeling strategy
Authors: Cheung, Jason K.; Shen, Vincent K.; Errington, Jeffrey R.; Truskett, Thomas M.
Serial title: AIChE Annual Meeting, Conference Proceedings
Abbreviated serial title: AIChE Annu. Meet. Conf. Proc.
Monograph title: 05AIChE: 2005 AIChE Annual Meeting and Fall Showcase, Conference Proceedings
Publication year: 2005
Pages: p 600
Language: English
Document type: Conference article (CA)
Conference name: 05AIChE: 2005 AIChE Annual Meeting and Fall Showcase
Conference date: Oct 30-Nov 4 2005
Conference location: Cincinnati, OH, United States
Conference code: 66925
Publisher: American Institute of Chemical Engineers, New York, NY 10016-5991, United States
Abstract: Understanding the environmental factors that reduce the stability of native-state proteins and induce non-native protein aggregation processes in solution is a challenge of great practical and technological importance. Protein aggregation has been linked to numerous human pathologies such as Alzheimer's and Huntington's diseases. It also leads to premature degradation of pharmaceutical formulations, severely restricting the available strategies for purification, storage, and delivery of therapeutic drugs. In this talk, we will discuss new simulations of a recently developed coarse-grained model [1] for protein solutions. The simulations employ a novel implementation of transition matrix Monte Carlo techniques introduced earlier (see, e.g., [2]) to probe how environmental stresses such as protein concentration, temperature, and hydrostatic pressure can induce unfolding and phase separation. Our results suggest that both single-molecule protein stability and the global phase behavior of protein solutions can be quite sensitive to basic protein sequence information (e.g., hydrophobic content). We will discuss these results in the context of experimental data, and we will also describe how this type of coarse-grained model [1] can give general insights into aggregation processes and phase behavior of complex fluids in aqueous solution.
Number of references: 2
Ei main heading: Proteins
Ei controlled terms: Phase equilibria - Environmental impact - Agglomeration - Diseases - Pathology - Monte Carlo methods
Uncontrolled terms: Phase stability - Pharmaceutical formulations - Protein stability - Coarse-grained models
Ei classification codes: 804.1 Organic Compounds - 531 Metallurgy and Metallography - 454.2 Environmental Impact & Protection - 802.3 Chemical Operations - 461.6 Medicine - 922.2 Mathematical Statistics
Treatment: Theoretical (THR); Experimental (EXP)
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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