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具有两个能够自主折叠的独立二级结构元件的二价肽的设计。

Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously.

作者信息

Pantoja-Uceda David, Pastor M Teresa, Salgado Jesús, Pineda-Lucena Antonio, Pérez-Payá Enrique

机构信息

Department of Medicinal Chemistry, Centro de Investigación Príncipe Felipe, Avda Autopista del Saler, 16. Valencia, Spain.

出版信息

J Pept Sci. 2008 Jul;14(7):845-54. doi: 10.1002/psc.1015.

DOI:10.1002/psc.1015
PMID:18247449
Abstract

This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (alpha-helix and beta-hairpin) and independent secondary-structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization by NMR revealed that the peptides were stable and did not show any long-range NOE interactions between the N-terminal beta-hairpin and the C-terminal alpha-helix. These results suggest that the two elements of secondary structure are stable and well folded.

摘要

本文描述了一种从头设计开始开发含有两种不同(α-螺旋和β-发夹)且独立二级结构元件的双价肽的策略。该设计基于使用构象受限肽库。通过核磁共振进行的结构表征表明,这些肽是稳定的,并且在N端β-发夹和C端α-螺旋之间未显示出任何长程核Overhauser效应(NOE)相互作用。这些结果表明,二级结构的两个元件是稳定且折叠良好的。

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