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    A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models

    Year: 2022

    Journal: Membranes, Volume 12, DEC

    Authors: Giordani, Cristiano; Russo, Stefano; Torrisi, Cristina; Morante, Silvia; Castelli, Francesco; Sarpietro, Maria Grazia

    Organizations: University of Antioquia-Project [2020-39532]; Department of Pharmacy, Faculty of Pharmaceutical and Food Sciences, University

    Keywords: RH-23; anticancer peptide; DMPC; MLVs; langmuir minitrough; differential scanning calorimetry

    Investigation of the interaction between drugs and biomembrane models, as a strategy to study and eventually improve drug/substrate interactions, is a crucial factor in preliminary screening. Synthesized peptides represent a source of potential anticancer and theragnostic drugs. In this study, we investigated the interaction of a novel synthesized peptide, called RH-23, with a simplified dimyristoylphosphatidylcholine (DMPC) model of the cellular membrane. The interaction of RH-23 with DMPC, organized either in multilamellar vesicles (MLVs) and in Langmuir-Blodgett (LB) monolayers, was assessed using thermodynamic techniques, namely differential scanning calorimetry (DSC) and LB. The calorimetric evaluations showed that RH-23 inserted into MLVs, causing a stabilization of the phospholipid gel phase that increased with the molar fraction of RH-23. Interplay with LB monolayers revealed that RH-23 interacted with DMPC molecules. This work represents the first experimental thermodynamic study on the interaction between RH-23 and a simplified model of the lipid membrane, thus providing a basis for further evaluations of the effect of RH-23 on biological membranes and its therapeutic/diagnostic potential.
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