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用于小型、稳定平行β-折叠支架的大环设计策略。

Macrocyclic design strategies for small, stable parallel beta-sheet scaffolds.

作者信息

Freire Felix, Gellman Samuel H

机构信息

Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

出版信息

J Am Chem Soc. 2009 Jun 17;131(23):7970-2. doi: 10.1021/ja902210f.

Abstract

Pairs of short peptide strands can be induced to adopt an antiparallel beta-sheet secondary structure in aqueous solution via a macrocyclic constraint, as illustrated by many natural and designed peptides. We show that an analogous strategy is successful for creation of small units of parallel beta-sheet secondary structure in aqueous solution. Cyclization in this case requires nonpeptide segments for N-to-N and C-to-C interstrand linkage. Surprisingly, we find that only one of these segments needs to be preorganized.

摘要

如许多天然和设计肽所示,通过大环约束可诱导短肽链对在水溶液中形成反平行β-折叠二级结构。我们表明,类似的策略成功地在水溶液中创建了平行β-折叠二级结构的小单元。在这种情况下,环化需要非肽段用于链间N到N和C到C的连接。令人惊讶的是,我们发现这些段中只有一个需要预先构建。

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