Programme

P.37 -- Poster, NCTP-39

Date: Wednesday, 30-07-2014

Time: 14h00 - 15h30

Aggregation of peptides in the tube model with correlated sidechain orientations

Nguyen Ba Hung (1,2), Trinh Xuan Hoang (1)

(1) Insitude of Physics, VAST (2) Vietnam Military Medical University

The ability of proteins and peptides to aggregate and form toxic amyloid fibrils has been associated with a range of diseases including BSE (or madcow), Alzheimer's and Parkinson's Diseases. In this study, we investigate the the role of amino acid sequence in the aggregation propensity by using a modified tube model with a new procedure for hydrophobic interaction. In this model, the amino acid sidechains are not considered explicitly, but their orientations are taken into account in the formation of hydrophobic contact. Extensive Monte Carlo simulations for systems of short peptides are carried out with the use of parallel tempering technique. Our results show that the formation of amyloid-like beta-structures by small number of peptides strongly depends on the amino acid sequence. Correlation of sidechain orientations promotes elongation of protofibrils. Our study provides an insight into the principles of how the formation of amyloid can be adjusted by amino acid sequence.

Presenter: Nguyễn Bá Hưng