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由β-氨基酸修饰的淀粉样β肽片段形成螺旋带状结构。

Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment.

作者信息

Castelletto Valeria, Hamley Ian W, Hule Rohan A, Pochan Darrin

机构信息

Department of Chemistry, University of Reading, Whiteknights, Reading RG6 6AD, UK.

出版信息

Angew Chem Int Ed Engl. 2009;48(13):2317-20. doi: 10.1002/anie.200805500.

Abstract

An addition to the family: The introduction of beta-amino acid residues into a modified amyloid beta peptide fragment resulted in well-defined helical nanoribbons (see cryo-TEM image) comprising beta strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flow-aligning nematic phase at higher concentration. The beta-strand nanoribbon structure is an addition to the known set of secondary structures adopted by beta-peptides.

摘要

家族新成员

将β-氨基酸残基引入修饰的淀粉样β肽片段中,产生了结构明确的螺旋纳米带(见图1中的低温透射电子显微镜图像),其包含主要垂直于纳米带轴取向的β链。在较高浓度下,纳米带排列成流动取向的向列相。β链纳米带结构是β肽所采用的已知二级结构集合中的新成员。

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