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Effect of Ca2+ on the secondary structure of linear and cyclic collagen sequence analogs.

Abstract：

:To investigate the role of secondary structure in the substrate specificity of human 72 kDa type IV collagenase, we synthesised linear and cyclic collagen sequence analogs. As Ca2+ plays a crucial role in the enzyme activity, the CD and FTIR spectra of the peptides were also measured in the presence of Ca2+. Most of the linear, but none of the cyclic peptides form stable 1:1 Ca2+ complexes. The cyclic hexapeptides adopt significantly different backbone conformations comprising not only beta-turns but also the less frequent gamma-turns. Consequently, in the cyclopeptides the scissile Gly-Ile(Leu) bond is embedded into a different conformational environment, but in spite of that none of them is a substrate or an inhibitor of the enzyme. The best substrate Ac-Pro-Leu-Gly-Leu-Ala-Gly-D-Lys-OH binds Ca2+, but does not form a stable 1:1 Ca2+ complex, which suggests that instead of a folded structure an extended flexible conformation is preferred by the enzyme.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Likó Z,Botyánszki J,Bódi J,Vass E,Majer Z,Hollósi M,Süli-Vargha H

doi

10.1006/bbrc.1996.1512

subject

Has Abstract

pub_date

1996-10-14 00:00:00

pages

351-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(96)91512-0

journal_volume

227

pub_type

杂志文章

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