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

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

Acta Biochimica Polonica

2004

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.

Governing the monomer-dimer ratio of human cystatin c by single amino acid substitution in the hinge region

100%

Szymańska A., Radulska A., Czaplewska P., Grubb A., Grzonka Z., Rodziewicz-Motowidło S.

Acta Biochimica Polonica

2009

vol. 56

issue 3

455-463

Three dimensional domain swapping is one of the mechanisms involved in formation of insoluble aggregates of some amyloidogenic proteins. It has been proposed that proteins able to swap domains may share some common structural elements like conformationally constrained flexible turns/loops. We studied the role of loop L1 in the dimerization of human cystatin C using mutational analysis. Introduction of turn-favoring residues such as Asp or Asn into the loop sequence (in position 57) leads to a significant reduction of the dimer fraction in comparison with the wild type protein. On the other hand, introduction of a proline residue in position 57 leads to efficient dimer formation. Our results confirm the important role of the loop L1 in the dimerization process of human cystatin C and show that this process can be to some extent governed by single amino acid substitution.

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.

Acta Biochimica Polonica

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.

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3 Acta Biochimica Polonica

1 2009

1 2004

1 2001

3 Grubb A.

3 Grzonka Z.

2 Kasprzykowski F.

2 Rodziewicz-Motowidło S.

2 Łankiewicz L.

1 Ciarkowski J.

1 Czaplewska P.

1 Drabik P.

1 Jankowska E.

1 Janowski R.

1 Jaskólski M.

1 Kasprzykowska R.

1 Kozak M.

1 Radulska A.

1 Sosnowska R.

1 Stachowiak K.

1 Szymańska A.

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.

Governing the monomer-dimer ratio of human cystatin c by single amino acid substitution in the hinge region

Structural studies of cysteine proteases and their inhibitors.