Role of water in protein aggregation and amyloid polymorphism.

作者: John E. Straub , Govardhan Reddy , D. Thirumalai

DOI: 10.1021/AR2000869

关键词:

摘要: A variety of neurodegenerative diseases are associated with amyloid plaques, which begin as soluble protein oligomers but develop into amyloid fibrils. Our incomplete understanding of this process underscores the need to decipher the principles governing protein aggregation. Mechanisms of in vivo amyloid formation involve a number of coconspirators and complex interactions with membranes. Nevertheless, understanding the biophysical basis of simpler in vitro amyloid formation is considered important for discovering ligands …

参考文章(57)
Charles L. Stevens, Max A. Lauffer, POLYMERIZATION-DEPOLYMERIZATION OF TOBACCO MOSAIC VIRUS PROTEIN. IV. THE ROLE OF WATER. Biochemistry. ,vol. 4, pp. 31- 37 ,(1965) , 10.1021/BI00877A007
S. Vaitheeswaran, D. Thirumalai, Hydrophobic and ionic interactions in nanosized water droplets. Journal of the American Chemical Society. ,vol. 128, pp. 13490- 13496 ,(2006) , 10.1021/JA063445H
Robert Tycko, Insights into the Amyloid Folding Problem from Solid-State NMR Biochemistry. ,vol. 42, pp. 3151- 3159 ,(2003) , 10.1021/BI027378P
Brandon H. Toyama, Mark J. S. Kelly, John D. Gross, Jonathan S. Weissman, The structural basis of yeast prion strain variants Nature. ,vol. 449, pp. 233- 237 ,(2007) , 10.1038/NATURE06108
G. Reddy, J. E. Straub, D. Thirumalai, Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires Proceedings of the National Academy of Sciences of the United States of America. ,vol. 107, pp. 21459- 21464 ,(2010) , 10.1073/PNAS.1008616107
R. I. Dima, D. Thirumalai, Probing the instabilities in the dynamics of helical fragments from mouse PrPc Proceedings of the National Academy of Sciences of the United States of America. ,vol. 101, pp. 15335- 15340 ,(2004) , 10.1073/PNAS.0404235101
Mai Suan Li, Nguyen Truong Co, Govardhan Reddy, Chin-Kun Hu, J. E. Straub, D. Thirumalai, Factors Governing Fibrillogenesis of Polypeptide Chains Revealed by Lattice Models Physical Review Letters. ,vol. 105, pp. 218101- ,(2010) , 10.1103/PHYSREVLETT.105.218101
Kimberly L. Sciarretta, David J. Gordon, Aneta T. Petkova, Robert Tycko, Stephen C. Meredith, Abeta40-Lactam(D23/K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry. ,vol. 44, pp. 6003- 6014 ,(2005) , 10.1021/BI0474867
Giovanni Bellesia, Joan-Emma Shea, What Determines the Structure and Stability of KFFE Monomers, Dimers, and Protofibrils? Biophysical Journal. ,vol. 96, pp. 875- 886 ,(2009) , 10.1016/J.BPJ.2008.10.040