Synthesis and structural characterization of helix-forming β-peptides:: trans-2-aminocyclopentanecarboxylic acid oligomers

被引：231

作者：

Appella, DH ^{[1
]}

Christianson, LA ^{[1
]}

Klein, DA ^{[1
]}

Richards, MR ^{[1
]}

Powell, DR ^{[1
]}

Gellman, SH ^{[1
]}

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1999年 / 121卷 / 33期

关键词：

D O I：

10.1021/ja991185g

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Synthetic protocols and circular dichroism (CD) spectra are reported for a series of oligomers of (R,R)-trans-2-aminocyclopentanecarboxylic acid (trans-ACPC). The two longest oligomers, a hexamer and an octamer, have also been examined crystallographically. Both crystal structures shaw that the beta-peptide backbone adopts a regular helix that is defined by a series of interwoven 12-membered ring hydrogen bonds ("12-helix"). Each hydrogen bond links a carbonyl oxygen to an amide proton three residues toward the C-terminus. CD data suggest that the conformational preference of trans-ACPC oligomers in methanol is strongly length-dependent, which implies that 12-helix formation is a cooperative process, as seen for the alpha-helix formed by conventional peptides. Previous work has established that oligomers and polymers of beta-amino acids can adopt helical conformations, but the 12-helix is an unprecedented beta-peptide secondary structure.

引用

页码：7574 / 7581

页数：8

共 60 条

[1]

[Anonymous], SHELXTL VERSION 5 RE

[2] Synthesis and characterization of trans-2-aminocyclohexanecarboxylic acid oligomers:: An unnatural helical secondary structure and implications for β-peptide tertiary structure [J].