Effect of antisense peptide binding on the dimerization of human cystatin C--gel electrophoresis and molecular modeling studies

Acta Biochim Pol. 2004;51(1):153-60.

Abstract

Human cystatin C (HCC) shows a tendency to dimerize. This process is particularly easy in the case of the L68Q HCC mutant and might lead to formation of amyloid deposits in brain arteries of young adults. Our purpose was to find ligands of monomeric HCC that can prevent its dimerization. Eleven antisense peptide ligands of monomeric HCC were designed and synthesized. The influence of these ligands on HCC dimerization was studied using gel electrophoresis and molecular modeling methods. The results suggest that all the designed peptides interact with monomeric HCC facilitating its dimerization rather than preventing it.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Amyloid / metabolism
  • Antisense Elements (Genetics) / chemistry*
  • Base Sequence
  • Binding Sites
  • Cerebral Arteries / metabolism
  • Cerebral Arteries / pathology
  • Cystatin C / chemistry*
  • Cystatin C / genetics
  • Cystatins / chemistry
  • Dimerization
  • Humans
  • Ligands
  • Models, Molecular
  • Protein Conformation
  • Young Adult

Substances

  • Amyloid
  • Antisense Elements (Genetics)
  • Cystatin C
  • Cystatins
  • L68Q cystatin C
  • Ligands