Differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC) techniques have been used to describe physicochemical properties of polypeptide LL-37. LL-37 is a 37-residue, amphipathic, helical peptide, the only cathelicidin-derived antimicrobial peptide found in the human organism. Thermal stability of the LL-37 peptide in a water solution was measured by DSC over the 288.15–333.15 K range. Furthermore, the ITC method supported by theoretical calculations (peptide–ligand docking) were used to study the interactions between LL-37 and some divalent metal ions, namely Cu2+, Zn2+, and Ni2+ ions as well as acetylsalicylic acid, ascorbic acid, and caffeine molecules. It has been proven that under experimental conditions, the LL-37 peptide reveals affinity only toward Cu2+ and Zn2+ ions. The stoichiometry, conditional binding constants, logKITC, and thermodynamic parameters (∆ITCG, ∆ITCH, T∆ITCS) of the resulting Cu(II) and Zn(II) complexes were determined and discussed.
Mendeley helps you to discover research relevant for your work.
CITATION STYLE
Makowska, J., Wyrzykowski, D., Kamysz, E., Tesmar, A., Kamysz, W., & Chmurzyński, L. (2019). Probing the binding selected metal ions and biologically active substances to the antimicrobial peptide LL-37 using DSC, ITC measurements and calculations. Journal of Thermal Analysis and Calorimetry, 138(6), 4523–4529. https://doi.org/10.1007/s10973-019-08310-9