Relationship between salt-bridge identity and 14-helix stability of β3-peptides in aqueous buffer

被引:21
作者
Guarracino, DA [1 ]
Chiang, HJR
Banks, TN
Lear, JD
Hodsdon, ME
Schepartz, A
机构
[1] Yale Univ, Dept Chem, New Haven, CT 06520 USA
[2] Yale Univ, Dept Mol Biophys, New Haven, CT 06520 USA
[3] Yale Univ, Dept Biochem, New Haven, CT 06520 USA
[4] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[5] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA
[6] Yale Sch Med, Dept Lab Med, New Haven, CT 06510 USA
关键词
D O I
10.1021/ol0527532
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
We report a systematic analysis of the relationship between salt bridge composition and 14-helix structure within a family of model beta-peptides in aqueous buffer. We find an inverse relationship between side-chain length and the extent of 14-helix structure as judged by CID. Introduction of a stabilizing salt bridge pair within a previously reported beta-peptide ligand for hDM2 led to changes in structure that were detectable by NMR.
引用
收藏
页码:807 / 810
页数:4
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