Program

P.7 -- Poster, IWTCP-3

Date: Wednesday, 29 July 2015

Time: 08h30 - 10h00

Effect of Taiwan mutation (D7H) on structures of amyloid beta peptides: replica exchange molecular dynamics study

Phan Minh Truong (1), Man Hoang Viet (2), Phuong H. Nguyen (3), Chin-Kun Hu (4), and Mai Suan Li (1,2)

(1) Institute for Computational Science and Technology, Ho Chi Minh City, Vietnam; (2) Institute of Physics, Polish Academy of Sciences, Warsaw, Poland ; (3) Universite Paris 7, Paris, France; (4) Institute of Physics, Academia Sinica, Taipei 11529, Taiwan.

Recent experiments have shown that the Taiwan mutation (D7H) slows down the fibril formation of amyloid peptides Aβ40 and Aβ42. Motivated by this finding we have studied the influence of D7H mutation on structures of Aβ peptides using the replica exchange molecular dynamics simulations with OPLS force field and implicit water model. Our study reveals that the mechanism behind modulation of aggregation rates is associated with decrease of beta-content and dynamics of the salt bridge D23-K28. Estimating the bending free energy of this salt bridge we have found that, in agreement with the experiments, the fibril formation rate of both peptides Aβ40 and Aβ42 is reduced about two times by mutation.

Presenter: Phan Minh Trường