Amyloid-like fibril-forming supramolecular β-sheets from a β-turn forming tripeptide containing non-coded amino acids:: the crystallographic signature

被引：26

作者：

Banerjee, A ^{[1
]}

Maji, SK

Drew, MGB

Haldar, D

Banerjee, A ^{[1
]}

机构：

[1] Indian Assoc Cultivat Sci, Dept Biol Chem, Kolkata 700032, W Bengal, India

[2] Univ Reading, Dept Chem, Reading RG6 6AD, Berks, England

来源：

TETRAHEDRON LETTERS | 2003年 / 44卷 / 02期

基金：

英国工程与自然科学研究理事会;

关键词：

beta-turn; Aib; beta-Ala; beta-sheet; amyloid fibrils;

D O I：

10.1016/S0040-4039(02)02570-4

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

The crystal structure of a terminally protected tripeptide Boc-Leu-Aib-beta-Ala-OMe 1 containing non-coded amino acids reveals that it adopts a beta-turn structure, which sell-assembles to form a supramolecular beta-sheet via non-covalent interactions. The SEM image of peptide 1 exhibits amyloid-like fibrillar morphology in the solid state. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：335 / 339

页数：5

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