Cyclooligomerization of a helix-bearing template into macrocycles bearing multiple helices

• 全文链接
• 请求原文

作   者：

Beyer RL;  Singh Y;  Fairlie DP; 

作者机构：

Inst Mol Biosci;  Ctr Drug Design & Dev;  Brisbane;  Qld 4072;  Univ Queensland;  Australia; 

关键词：

PEPTIDES;  AMINO-ACIDS;  OXAZOLES;  THIAZOLE;  SECONDARY STRUCTURE;  LOOPS;  PROTEINS;  CONFORMATIONS;  WATER; 

期刊名称：

Organic letters

i s s n：

1523-7060

年卷期：

2008 年 10 卷 16 期

页   码：

3481-3484

页   码：

摘   要：

Cyclooligomerization was investigated for separating and spatially arranging helical peptides as discontinuous surfaces. Tetrapeptide H-[Ile-Ser-Lys(Ox)]-OH, containing a turn-inducing oxazole constraint, was connected through its lysine side chain via a beta-alanine linker to the C-terminus of a two-turn helical nonapeptide Ac-(cyclo-4,8)-LRL [KARAD](Aib). The resulting helix-appended template was self-condensed and cyclized to a library of macrocycles (n = 2-6) containing multiple (2-6) helices. An NMR structure shows retention of alpha helicity in the cyclotrimer (n = 3).