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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 różnych reszt β-aminokwasowych na zdolności koordynacyjne peptydów wobec jonów metali przejściowych

Krzciuk-Gula Joanna, Ledwoń Patrycja, Staśkiewicz Agnieszka, Latajkа Rafał

Wiadomości Chemiczne

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2020

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[Z] 74, 3-4

285--310

EN

Peptidomimetics are different groups of compounds which are the modifications of natural occurring peptides - mostly in the sense of the structure. Due to these kind of changes, the new, modified systems are more stable and could act as a tool dedicated in specific biological activity. One of the most important and developed group of peptidomimetics are β-peptides. This review discusses the coordination ability of peptides containing β-amino acid residues incorporated into their sequence. Special attention is given to the importance of βAla residue and metal binding affinity of transition metal ions, especially Cu2+ ion. The coordination process occurs analogously to peptides composed of a-amino acids. The complexes are usually formed initially by coordination of N-terminal amine group and subsequently, with increasing pH value, by deprotonation of amide bonds. The main difference can be observed in the stability and geometry of complexes. Namely, the stability constants of β-peptides are usually slightly lower than in the case of natural analogues. Furthermore, the review presents data according to coordination ability of peptides containing β-amino acids, such as: βAsp, βHis, βCys and βLys. In spite of differences between standard peptides and their analogues, containing β-amino acid residues, there are no very important differences in the model of their coordination with the transition metal ions. However, the comparison of β-peptides and their natural counterparts reveals interesting features, which can be useful for more effective designing of new compounds possessing expected properties.

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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].