- 作者: David M. Morgana, David G. Lynna*, Ami S. Lakdawalab, James P. Snyderb and Dennis C. Liottab
- 作者服務機構: Departments of Chemistry and Biology, Emory University, 1515 Pierce Drive, Atlanta, Ga 30322, U.S.A.
- 中文摘要: In celebration of the many contributions to peptide chemistry from K.-T. Wang’s laboratory, this manuscript explores the structure of the Ab(10-35) fibril. This central segment of the Ab peptide of Alzheimer’s Disease self-assembles into well-ordered paracrystalline arrays that seem to contradict many of the accepted paradigms established for soluble, globular proteins. Here we exploit initial molecular modeling efforts to assist in understanding these apparent contradictions. The emerging structure is one of a large self-assembly of b-strands, whose stability is dependent on large spatial and temporal fluctuation about a central core, giving rise to what can be best described as a dynamic and fluid tube-like micelle. This fibril structure maintains features that are distinctly different from those of either synthetic or biological fibrils, and these differences have profound implications for biomedical intervention in amyloid diseases as well as for the design of self-assembling nanoscale fibrils.
- 英文摘要: --
- 中文關鍵字: Molecular dynamics; Parallel b-sheets; Amyloid structure; H-bonds.
- 英文關鍵字: Molecular dynamics; Parallel b-sheets; Amyloid structure; H-bonds.