The publication reviews the results on the tyrosinase inhibition capacity of a short peptide and peptide conjugates with known low molecular weight inhibitors of this enzyme. Tyrosinase is a widespread copper-dependent enzyme capable of catalyzing two reaction pathways for oxidizing monophenols to o-diphenols and o-diphenols to o-quinones. Despite the wide distribution in nature, the peptide chain that builds the catalytic cavity is relatively highly conserved for all organisms. As the research results collected in the work show, the creation of short peptide conjugates with known tyrosinase inhibitors, such as kojic acid, significantly reduces the toxicity of the inhibitor and improves its stability.
The interests of the research group working under the supervision of professor Rafał Latajka at the Department of Bioorganic Chemistry at the Wrocław University of Science and Technology are focused on several projects in the field of biological chemistry. Regardless of whether a given project concerns – the synthesis and activity of new enzyme inhibitors, peptides, peptidomimetics, or aromatic foldamers – the thread of correlation between the structure and activity of the studied systems always plays a pivotal role. In this article we are presenting current projects in our research group.
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