Effect of antisense peptide binding on the dimerization of human cystatin C--gel electrophoresis and molecular modeling studies.
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.
Stachowiak
Krystyna
K
Faculty of Chemistry, University of Gdańsk, Gdańsk, Poland. krysias@chemik.chem.univ.gda.pl
Rodziewicz-Motowidło
Sylwia
S
Sosnowska
Renata
R
Kasprzykowski
Franciszek
F
Łankiewicz
Leszek
L
Grubb
Anders
A
Grzonka
Zbigniew
Z
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000682:Amyloid / Q000378:metabolism; D016375:Antisense Elements (Genetics) / Q000737:chemistry*; D001483:Base Sequence; D001665:Binding Sites; D002536:Cerebral Arteries / Q000378:metabolism / Q000473:pathology; D055316:Cystatin C / Q000737:chemistry* / Q000235:genetics; D015891:Cystatins / Q000737:chemistry; D019281:Dimerization; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation; D055815:Young Adult
D000682:Amyloid; D016375:Antisense Elements (Genetics); D055316:Cystatin C; D015891:Cystatins; C085910:L68Q cystatin C; D008024:Ligands