Research

In the Laboratory of Bioorganic Chemistry research on synthetic inhibitors of serine proteinases are continued since the mid-1980s. The first, base structures we used to design inhibitors of this family of enzymes were CMTI-I and CMTI-III inhibitors isolated from pumpkin seeds. Another was the trypsin inhibitor SFTI-1 isolated from sunflower seeds. The search for selective inhibitors of serine proteinases includes the classical chemical synthesis of peptides on a solid support and in solution, including the use of combinatorial chemistry methods, as well as the study of their interactions with selected proteinases using kinetic methods.

New directions of research in our Laboratory are:

• design, chemical synthesis and evaluation of specificity of peptide inhibitors of proteasome, matriptase-1, matriptase-2 and furin;
• study of the mechanism of peptide splicing;
• antimicrobial peptides;
• peptide conjugates;
• increase of peptides bioavailability;