ORIGINAL RESEARCH article
Front. Mol. Biosci.
Sec. Protein Biochemistry for Basic and Applied Sciences
Volume 12 - 2025 | doi: 10.3389/fmolb.2025.1593661
The interaction of Cu(II) and Zn(II) with peptide fragment of HSPB1 and its analogs
Provisionally accepted
- 1Institute of Health Sciences, University of Opole, Opole, Poland
- 2University of Naples Federico II, Naples, Campania, Italy
- 3National University of Pharmacy, Kharkov, Kharkiv Oblast, Ukraine
- 4Medical University of Lublin, Lublin, Lublin, Poland
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Copper (II) and zinc (II) ions are essential microelements in the human body, interacting with numerous biologically active molecules, including proteins and peptides. The precise identification of binding sites, complete with the detailed characterization of binding amino acid residues, is of great importance. This is particularly significant in the context of uncovering the mechanisms of diseases associated with single nucleotide polymorphisms (SNPs), and consequently, developing effective treatments.This study highlights the importance of His-131 and Glu-126 residues in Cu 2+ and Zn 2+ ion binding by peptide fragments of the HSPB1 protein. These residues are essential for both the stability of the complexes and the nature of their interaction with the metal ions. Analytical methods exploring complexation behavior across a pH range of 2-10 and in buffer solutions provide a comprehensive view of the thermodynamic properties of the studied systems. This enables the prediction of their behavior under diverse conditions.
Keywords: Copper, Zinc, Heat shock proteins, Peptides, Ala-screening
Received: 14 Mar 2025; Accepted: 23 Jul 2025.
Copyright: © 2025 Szebesczyk, Musumeci, Napolitano, Kukhtenko and Iwaniak. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Agnieszka Szebesczyk, Institute of Health Sciences, University of Opole, Opole, Poland
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