用于形成超分子肽双螺旋的新型分子支架：晶体学见解

A new molecular scaffold for the formation of supramolecular peptide double helices: the crystallographic insight.

作者信息

Guha Samit, Drew Michael G B, Banerjee Arindam

机构信息

Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.

出版信息

Org Lett. 2007 Mar 29;9(7):1347-50. doi: 10.1021/ol0701870. Epub 2007 Mar 9.

DOI:10.1021/ol0701870

PMID:17346055

Abstract

[structure: see text]. A series of water-soluble synthetic dipeptides (1-3) with an N-terminally located beta-alanine residue, beta-alanyl-l-valine (1), beta-alanyl-l-isoleucine (2), and beta-alanyl-l-phenylalanine (3), form hydrogen-bonded supramolecular double helices with a pitch length of 1 nm, whereas the C-terminally positioned beta-alanine containing dipeptide (4), l-phenylalanyl-beta-alanine, does not form a supramolecular double helical structure. beta-Ala-Xaa (Xaa = Val/Ile/Phe) can be regarded as a new motif for the formation of supramolecular double helical structures in the solid state.

摘要

[结构：见正文]。一系列N端带有β-丙氨酸残基的水溶性合成二肽（1-3），β-丙氨酰-L-缬氨酸（1）、β-丙氨酰-L-异亮氨酸（2）和β-丙氨酰-L-苯丙氨酸（3），形成了螺距为1 nm的氢键超分子双螺旋结构，而C端含β-丙氨酸的二肽（4），L-苯丙氨酰-β-丙氨酸，则不形成超分子双螺旋结构。β-Ala-Xaa（Xaa = Val/Ile/Phe）可被视为固态下形成超分子双螺旋结构的新基序。