Cooperative Effect of the Two Hydrogen Bonding Types on 11/9-Helical Folding of α/β-Peptides

被引：3

作者：

Jang, Geunhyuk ^{[1
]}

Lee, Mihye ^{[1
]}

Lee, Jaeyeon ^{[1
]}

Shim, Jihyun ^{[1
]}

Kang, Philjae ^{[1
]}

Choi, Moon-Gun ^{[1
]}

Choi, Soo Hyuk ^{[1
]}

机构：

[1] Yonsei Univ, Dept Chem, Seoul 03722, South Korea

来源：

BULLETIN OF THE KOREAN CHEMICAL SOCIETY | 2018年 / 39卷 / 02期

关键词：

alpha/beta-peptide; Helix; Hydrogen bonding; Crystal structure; BETA HYBRID PEPTIDES; STRUCTURAL-CHARACTERIZATION; AMINO ACIDS; HELIX TYPES; DEPSIPEPTIDES; DERIVATIVES; FOLDAMERS; CRYSTALS; PROTEINS; RING;

D O I：

10.1002/bkcs.11376

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

alpha/beta-Peptide 11/9-helix is an unconventional helical structure in which 11- and 9-membered ring hydrogen bonds alternate along the helical axis. We have examined the interplay and the relative strength of these two hydrogen bonding types by IR, NMR, and X-ray crystallographic methods. A pair of two adjacent hydrogen bonds with opposite directionality cooperatively stabilized each other in non-hydrogen-bonding solvents. In contrast, an unpaired hydrogen bond was unstable to promote helical folding. The IR and the NMR data of alpha/beta-depsipeptides suggested that a 9-membered ring hydrogen bond is favored over an 11-membered ring hydrogen bond.

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页码：244 / 249

页数：6

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