Abstract
A peptide -m
, which is a fragment from residue 21 to residue 31 of
-microgloblin, is experimentally known to self-assemble and form amyloid fibrils. In order to analyze the conformations of amyloid-forming peptides in the early stage of aggregation, we applied the replica-exchange molecular dynamics method to the system consisting of three fragments of
-m
. From the analyses concerned with the temperature dependence, we found that there is a clear transition temperature in which the peptides aggregate each other. Moreover, we found that there are two major stable states: One of them is like amyloid fibrils and the other is amorphous aggregates by the free energy analyses.
Notes
No potential conflict of interest was reported by the authors.