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1

Antibacterial peptides of the moth Galleria mellonella

100%

Mak P., Chmiel D., Gacek G. J.

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2001

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vol. 48

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issue 4

1191-1195

EN

The work describes purification and biochemical characterization of two inducible antimicrobial peptides from the hemolymph of Galleria mellonella. The peptides were isolated by a sequence of reversed-phase chromatography steps from the hemolymph of larvae immunized with viable bacteria. The first peptide is a member of the cecropin family while the second one is rich in proline residues and has a unique sequence.

2

Modes of inhibition of cysteine proteases.

100%

Rzychon M., Chmiel D., Stec-Niemczyk J.

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vol. 51

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issue 4

861-873

EN

Cysteine proteases are involved in many physiological processes and their hyperactivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic centre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a similar mechanism, as well as inhibitors of the apoptosis protein family that bind in a direction opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.

3

New generation of peptide antibiotics

64%

Dubin A., Mak P., Dubin G., Rzychon M., Stec-Niemczyk J., Wladyka B., Maziarka K., Chmiel D.

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2005

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vol. 52

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issue 3

633-638

EN

The increasing antibiotic resistance of pathogenic bacteria calls for the development of alternative antimicrobial strategies. Possible approaches include the development of novel, broad-spectrum antibiotics as well as specific targeting of individual bacterial virulence factors. It is impossible to decide currently which strategy will prove more successful in the future since they both promise different advantages, but also introduce diverse problems. Considering both approaches, our laboratory's research focuses on the evaluation of hemocidins, broad-spectrum antibacterial peptides derived from hemoglobin and myoglobin, and staphostatins, specific inhibitors of staphopains - Staphylococcus aureus secreted proteases that are virulence factors regarded as possible targets for therapy. The article summarizes recent advances in both fields of study and presents perspectives for further development and possible applications.

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3 Acta Biochimica Polonica

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3 Chmiel D.

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Antibacterial peptides of the moth Galleria mellonella

Modes of inhibition of cysteine proteases.

New generation of peptide antibiotics