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

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

Research output: Contribution to journalArticle

6 Citations (Scopus)

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 β-turns but also the less frequent γ-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.

Original languageEnglish
Pages (from-to)351-359
Number of pages9
JournalBiochemical and biophysical research communications
Volume227
Issue number2
DOIs
Publication statusPublished - Oct 14 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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