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)


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
Issue number2
Publication statusPublished - Oct 14 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Effect of Ca<sup>2+</sup> on the secondary structure of linear and cyclic collagen sequence analogs'. Together they form a unique fingerprint.

  • Cite this