Molecular dynamics study of amyloid formation of two Abl-SH3 domain peptides

被引：7
作者：
Liepina, Inta [1 ]
Ventura, Salvador
Czaplewski, Cezary
Liwo, Adam
机构：
[1] Latvian Inst Organ Synth, LV-1006 Riga, Latvia
[2] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, E-08193 Barcelona, Spain
[3] Univ Gdansk, Fac Chem, PL-80952 Gdansk, Poland
来源：
JOURNAL OF PEPTIDE SCIENCE | 2006年 / 12卷 / 12期
关键词：
amyloid; amyloid peptides; amyloid formation; molecular dynamics; beta-sheet;
D O I：
10.1002/psc.813
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Molecular dynamics (MD) simulations were carried out for two-strand and ten-strand beta-sheets constructed from two peptides corresponding to the diverging turn of two homologous Ab1-SH3 domains, DLSFMKGE (MK; from Drosophila) and DLSFKKGE (KK; from man), in explicit water at the temperatures of 30, 170/190 and 300 K. It was found that the 2 x MK beta-sheet is more stable than the 2 x KK beta-sheet, and that the 10 x MK beta-sheet is more stable than the 10 x KK beta-sheet; this suggests that the MK systems are fibril-creating and the KK systems are not. These results might explain why most SH3 domains possess two conserved basic residues at the diverging turn, which may act as gatekeepers in order to avoid aggregation. Copyright (c) 2006 European Peptide Society and John Wiley & Sons, Ltd.
引用
收藏
页码：780 / 789
页数：10
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