Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates
Isothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopy, and molecular dynamics simulations were applied to describe interactions between lipopeptides and decavanadate ions ([V<sub>10</sub>O<sub>28</sub>]<sup>6−</sup>). The selected lipopeptid...
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2025-04-01
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| author | Martyna Kapica Elżbieta Kamysz Ola Grabowska Aleksandra Tesmar Marek Pająk Katarzyna Chmur Jakub Brzeski Sergey A. Samsonov Dariusz Wyrzykowski |
| author_facet | Martyna Kapica Elżbieta Kamysz Ola Grabowska Aleksandra Tesmar Marek Pająk Katarzyna Chmur Jakub Brzeski Sergey A. Samsonov Dariusz Wyrzykowski |
| author_sort | Martyna Kapica |
| collection | DOAJ |
| description | Isothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopy, and molecular dynamics simulations were applied to describe interactions between lipopeptides and decavanadate ions ([V<sub>10</sub>O<sub>28</sub>]<sup>6−</sup>). The selected lipopeptides are conjugates of the amide of the KR12 peptide, the smallest antimicrobial peptide derived from human cathelicidin LL-37, with lauric acid (C12-KR12) and myristic acid (C14-KR12). The smaller sizes of C12-KR12 and C14-KR12 compared to proteins allow for the rigorous characterization of their non-covalent interactions with highly negatively charged [V<sub>10</sub>O<sub>28</sub>]<sup>6−</sup> ions. The stoichiometry of the resulting decavanadate–peptide complexes and the thermodynamic parameters (Δ<i>G</i>, Δ<i>H</i>, and TΔ<i>S</i>) of the interactions were determined. The ITC results, supported by the MD simulation, showed that the binding of cationic lipopeptides for decavanadate is rather non-specific and is driven by enthalpic contributions resulting from electrostatic interactions between the positively charged residues of the peptides and the anionic decavanadate. Furthermore, the influence of temperature and the interactions with decavanadate ions on the stability of the α-helical structure of the lipopeptides were assessed based on CD spectra. Under the experimental conditions (50 mM sodium cacodylate buffer, pH 5), the peptides adopt an α-helical conformation, with C14-KR12 showing greater thermal stability. The interactions with vanadium species disrupt the α-helical structure and reduce its thermal stability. |
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| issn | 1420-3049 |
| language | English |
| publishDate | 2025-04-01 |
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| spelling | doaj-art-6aef7baf645249868e01dbe210403c552025-08-20T02:09:17ZengMDPI AGMolecules1420-30492025-04-01307158910.3390/molecules30071589Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with PolyoxidovanadatesMartyna Kapica0Elżbieta Kamysz1Ola Grabowska2Aleksandra Tesmar3Marek Pająk4Katarzyna Chmur5Jakub Brzeski6Sergey A. Samsonov7Dariusz Wyrzykowski8Faculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandDepartment of Physical and Biocoordination Chemistry, Medical University of Lodz, Muszyńskiego 1, 90-151 Lodz, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-308 Gdańsk, PolandIsothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopy, and molecular dynamics simulations were applied to describe interactions between lipopeptides and decavanadate ions ([V<sub>10</sub>O<sub>28</sub>]<sup>6−</sup>). The selected lipopeptides are conjugates of the amide of the KR12 peptide, the smallest antimicrobial peptide derived from human cathelicidin LL-37, with lauric acid (C12-KR12) and myristic acid (C14-KR12). The smaller sizes of C12-KR12 and C14-KR12 compared to proteins allow for the rigorous characterization of their non-covalent interactions with highly negatively charged [V<sub>10</sub>O<sub>28</sub>]<sup>6−</sup> ions. The stoichiometry of the resulting decavanadate–peptide complexes and the thermodynamic parameters (Δ<i>G</i>, Δ<i>H</i>, and TΔ<i>S</i>) of the interactions were determined. The ITC results, supported by the MD simulation, showed that the binding of cationic lipopeptides for decavanadate is rather non-specific and is driven by enthalpic contributions resulting from electrostatic interactions between the positively charged residues of the peptides and the anionic decavanadate. Furthermore, the influence of temperature and the interactions with decavanadate ions on the stability of the α-helical structure of the lipopeptides were assessed based on CD spectra. Under the experimental conditions (50 mM sodium cacodylate buffer, pH 5), the peptides adopt an α-helical conformation, with C14-KR12 showing greater thermal stability. The interactions with vanadium species disrupt the α-helical structure and reduce its thermal stability.https://www.mdpi.com/1420-3049/30/7/1589polyoxidometalatesvanadiumlipopeptidepeptide–ligand interactionsisothermal titration calorimetrymolecular dynamics |
| spellingShingle | Martyna Kapica Elżbieta Kamysz Ola Grabowska Aleksandra Tesmar Marek Pająk Katarzyna Chmur Jakub Brzeski Sergey A. Samsonov Dariusz Wyrzykowski Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates Molecules polyoxidometalates vanadium lipopeptide peptide–ligand interactions isothermal titration calorimetry molecular dynamics |
| title | Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates |
| title_full | Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates |
| title_fullStr | Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates |
| title_full_unstemmed | Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates |
| title_short | Interactions of Laurylated and Myristoylated KR12 Fragment of the LL37 Peptide with Polyoxidovanadates |
| title_sort | interactions of laurylated and myristoylated kr12 fragment of the ll37 peptide with polyoxidovanadates |
| topic | polyoxidometalates vanadium lipopeptide peptide–ligand interactions isothermal titration calorimetry molecular dynamics |
| url | https://www.mdpi.com/1420-3049/30/7/1589 |
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