Charge effects on the fibril-forming peptide KTVIIE: a two-dimensional replica exchange simulation study.

ABSTRACT: The assembly of peptides into ordered nanostructures is increasingly recognized as both a bioengineering tool for generating new materials and a critical aspect of aggregation processes that underlie neurological diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. There is a major problem in understanding how extremely subtle sequence changes can lead to profound and often unexpected differences in self-assembly behavior. To better delineate the complex interplay of different microscopic driving forces in such cases, we develop a methodology to quantify and compare the propensity of different peptide sequences to form small oligomers during early self-assembly stages. This umbrella-sampling replica exchange molecular dynamics method performs a replica excha

SUBMITTER: Jeon J 

PROVIDER: S-EPMC3328716 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature