The fourth helical secondary structure of β-peptides:: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

被引:88
作者
Gademann, K [1 ]
Häne, A [1 ]
Rueping, M [1 ]
Jaun, B [1 ]
Seebach, D [1 ]
机构
[1] Swiss Fed Inst Technol, Organ Chem Lab, CH-8093 Zurich, Switzerland
关键词
amino acids; beta-peptides; conformational analysis; peptidomimetics; secondary structure;
D O I
10.1002/anie.200250290
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Small change with great effect! An oligomer of α-hydroxy-β-amino acids folds into a right-handed helical structure (see picture) in MeOH; in contrast, the methyl analogue has a pleated sheet structure. Including this new helix, four different helical secondary structures of β-peptides have been discovered - a structural diversity that should allow the generation of elaborate proteomimetics.
引用
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页码:1534 / 1537
页数:4
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