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Interaction with the Surrounding Water Plays a Key Role in Determining the Aggregation Propensity of Proteins

Authors
Chong, Song-HoHam, Sihyun
Issue Date
Apr-2014
Publisher
WILEY-V C H VERLAG GMBH
Keywords
amyloid beta-peptides; hydrophobic effect; proteins; thermodynamics; water
Citation
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.53, no.15, pp 3961 - 3964
Pages
4
Journal Title
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume
53
Number
15
Start Page
3961
End Page
3964
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/10907
DOI
10.1002/anie.201309317
ISSN
1433-7851
1521-3773
Abstract
Understanding the molecular determinants of the relative propensities of proteins to aggregate in a cellular environment is a central issue for treating protein-aggregation diseases and developing peptide-based therapeutics. Despite the expectation that protein aggregation can largely be attributed to direct protein-protein interactions, a crucial role the surrounding water in determining the aggregation propensity of proteins both invitro and invivo was identified. The overall protein hydrophobicity, defined solely by the hydration free energy of a protein in its monomeric state sampling its equilibrium structures, was shown to be the predominant determinant of protein aggregation propensity in aqueous solution. Striking discrimination of positively and negatively charged residues by the surrounding water was also found. This effect depends on the protein net charge and plays a crucial role in regulating the solubility of the protein. These results pave the way for the design of aggregation-resistant proteins as biotherapeutics.
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