Macrocyclic Design Strategies for Small, Stable Parallel β-Sheet Scaffolds

Macrocyclic Design Strategies for Small, Stable Parallel β-Sheet Scaffolds
复制标题

DOI:
10.1021/ja902210f
复制
发表时间:
2009-06-17
影响因子:
15
通讯作者:
Gellman, Samuel H.
Gellman, Samuel H.
中科院分区:
化学1区
文献类型:
--
作者:
Freire, Felix;Gellman, Samuel H.

文献摘要

被引文献

相似文献

通过大环约束,可以诱导成对的短肽链在水溶液中采用反平行的β-折叠二级结构,如许多天然和设计的肽所示。我们表明,类似的策略可以成功地在水溶液中创建小单位的平行β-折叠二级结构。在这种情况下,环化需要非肽片段进行 N 至 N 和 C 至 C 链间连接。令人惊讶的是,我们发现这些部分中只有一个需要预先组织。
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.