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

Krystyna Stachowiak; Sylwia Rodziewicz-Motowidło; Renata Sosnowska; Franciszek Kasprzykowski; Leszek Łankiewicz; Anders Grubb; Zbigniew Grzonka

doi:10.18388/abp.2004_3607

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

Krystyna Stachowiak Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland. krysias@chemik.chem.univ.gda.pl;
Sylwia Rodziewicz-Motowidło
Renata Sosnowska
Franciszek Kasprzykowski
Leszek Łankiewicz
Anders Grubb
Zbigniew Grzonka

DOI: https://doi.org/10.18388/abp.2004_3607

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.

Published

2004-03-31

Issue

Vol. 51 No. 1 (2004)

Section

Articles

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