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Peptydy i peptydomimetyki jako inhibitory tyrozynazy

Ledwoń Patrycja, Jewgiński Michał, Latajka Rafał

Wiadomości Chemiczne

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2023

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[Z] 77, 5-6

411--423

EN

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.

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Peptydomimetyki i foldamery aromatyczne w chemii biologicznej

Ledwoń Patrycja, Staśkiewicz Agnieszka, Jewgiński Michał, Latajka Rafał

Wiadomości Chemiczne

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2022

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[Z] 76, 5-6

349--363

EN

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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Wpływ reszt ΔPhe na konformację łańcucha peptydowego

Ledwoń Patrycja, Staśkiewicz Agnieszka, Jewgiński Michał, Latajka Rafał

Wiadomości Chemiczne

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2020

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[Z] 74, 1-2

9--32

EN

In the past few years dehydropeptides have been highly investigated, mainly due to their biological activity: for instance, as antimicrobials or catalytic agents in some enzymes [1, 51-53]. In presented studies it was established that dehydrophenylalanine residue (ΔPhe) can be an interesting building block of various peptide chains, in order to control and modify a structure, conformation and function of the target molecule [3, 4, 5-7]. It was also pointed out that the length of a linker between dehydroamino acid residues (if two or more are present in a peptide chain) is a crucial factor in case of conformational dependence [23]. Short, one-residue spacers promote 310-helical structure, while longer ones increase the coexistence of 310-helical and α-helical conformers (Table 7). What is worth to notice, temperature or polarity of solvent can dramatically change the screw sense of obtained 310-helices (Table 11). Additionally, the screw sense can be altered by other variables, like chirality of C and N-terminus or dehydroamino acid isomer type (E or Z) [4-11]. Considering chain conformation, it can be disparate, depending on environment’s solid or liquid state (Table 7). Application of dehydropeptides is widely spread among assorted field of studies. As they can form a few self-assembled structures (e.g. nanotubes, nanovesicles or hydrogels), arise an opportunity of encapsulation of small drug molecules or trapping and releasing bioactive substances [47-49]. Sequences with incorporated dehydroamino acid residues were examined as a potential drug - interaction with negatively charged membrane of bacteria species is possible by virtue of positive polarization of peptide chain [51]. Part of the sequences exert an activity against E. coli, S. aureus, P. falciparum or highly dangerous MRSA, presenting versatile potential correlated with their secondary structure [50-53].