title: Effect of Taiwan mutation (D7H) on structures of amyloid-β peptides: replica exchange molecular dynamics study.
abstract: Recent experiments have shown that the Taiwan mutation (D7H) slows 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 peptide monomers 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 β-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.
authors.affiliation: Institute for Computational Science and Technology , SBI Building, Quang Trung Software City, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City, Vietnam.
authors.forename: Phan Minh
authors.initials: PM
authors.lastname: Truong
authors.forename: Man Hoang
authors.initials: MH
authors.lastname: Viet
authors.forename: Phuong H
authors.initials: PH
authors.lastname: Nguyen
authors.forename: Chin-Kun
authors.initials: CK
authors.lastname: Hu
authors.forename: Mai Suan
authors.initials: MS
authors.lastname: Li
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000235:genetics*; D004548:Elasticity; D056004:Molecular Dynamics Simulation; D009154:Mutation; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics*; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry; D013624:Taiwan; D014867:Water / Q000737:chemistry
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D012997:Solvents; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42); D014867:Water