Results found: 3

Number of results on page

Search results

Sort By:

Limit search:

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

100%

Stachowiak K., Rodziewicz-Motowidło S., Sosnowska R., Kasprzykowski F., Łankiewicz L., Grubb A., Grzonka Z.

vol. 51

issue 1

153-160

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.

Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.

100%

Drabik P., Politowska E., Czaplewski C., Kasprzykowski F., Łankiewicz L., Ciarkowski J.

2000

vol. 47

issue 4

1061-1066

Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.

Structural studies of cysteine proteases and their inhibitors.

68%

Grzonka Z., Jankowska E., Kasprzykowski F., Kasprzykowska R., Łankiewicz L., Wiczk W., Wieczerzak E., Ciarkowski J., Drabik P., Janowski R., Kozak M., Jaskólski M., Grubb A.

2001

vol. 48

issue 1

1-20

Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins.

Refine search results

3 Acta Biochimica Polonica

1 2004

1 2001

1 2000

3 Kasprzykowski F.

3 Łankiewicz L.

2 Ciarkowski J.

2 Drabik P.

2 Grubb A.

2 Grzonka Z.

1 Czaplewski C.

1 Jankowska E.

1 Janowski R.

1 Jaskólski M.

1 Kasprzykowska R.

1 Kozak M.

1 Politowska E.

1 Rodziewicz-Motowidło S.

1 Sosnowska R.

1 Stachowiak K.

1 Wiczk W.

1 Wieczerzak E.

Search results

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

Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.

Structural studies of cysteine proteases and their inhibitors.