Why Proline? Influence of Ring-Size on the Collagen Triple Helix

被引：21

作者：

Egli, Jasmine ^{[1
]}

Schnitzer, Tobias ^{[1
]}

Dietschreit, Johannes C. B. ^{[2
]}

Ochsenfeld, Christian ^{[2
]}

Wennemers, Helma ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Lab Organ Chem, Vladimir Prelog Weg 3, CH-8093 Zurich, Switzerland

[2] Univ Munich, Dept Chem, Chair Theoret Chem, Butenandtstr 7, D-81377 Munich, Germany

来源：

ORGANIC LETTERS | 2020年 / 22卷 / 02期

基金：

瑞士国家科学基金会;

关键词：

L-AZETIDINE-2-CARBOXYLIC ACID RESIDUE; CONFORMATIONAL STABILITY; CRYSTAL-STRUCTURE; AZETIDINE-2-CARBOXYLIC ACID; PROTEIN CONFORMATION; ANALOGS; ISOMERIZATION; DERIVATIVES;

D O I：

10.1021/acs.orglett.9b03528

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

The effect of four- and six-membered ring-size analogs (azetidine- and piperidine-2-carboxylic acid, H-Aze-OH and H-Pip-OH) of proline on the stability of the collagen triple helix was examined. Computational and nuclear magnetic resonance spectroscopic studies with model compounds and thermal denaturation experiments with collagen peptides showed that the ring-size analogs destabilize the triple helix to a similar extent by either mismatching backbone dihedral angles phi and psi (Pip) or by an unfavorable trans/cis amide bond ratio (Aze).

引用

页码：348 / 351

页数：4

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