Valorphins alter physicochemical characteristics of phosphatidylcholine membranes: Datasets on lipid packing, bending rigidity, specific electrical capacitance, dipole potential, vesicle size

Endogenous hemorphins are being intensively investi-gated as therapeutic agents in neuropharmacology, and also as biomarkers in mood regulation, inflammation and oncology. The datasets collected herein report physic-ochemical parameters of 1-palmitoyl-2-oleoyl-sn-glycero- 3-phosphocholine membranes in the presence of VV-hemorphin-5 (Val-Val-Tyr-Pro-Trp-Thr-Gln) and analogues, modified at position 1 and 7 by the natural amino acid isoleucine or the non-proteinogenic 2-aminoisobutyric, 2,3-diaminopropanoic or 2,4-diaminobutanoic amino acids. These peptides have been previously screened for nociceptive activ-ity and were chosen accordingly. The present article contains fluorescence spectroscopy data of Laurdan-and di-8-ANEPPS-labelled large unilamellar vesicles (LUV) providing the degree of hydration and dipole potential of lipid bilayers in the pres-ence of VV-hemorphin-5 analogues. Lipid packing is accessi-ble from Laurdan intensity profiles and generalized polariza-tion datasets reported herein. The data presented on fluores-cence intensity ratios of di-8-ANEPPS dye provide dipole po-tential values of phosphatidylcholine-valorphin membranes. Vesicle size and electrophoretic mobility datasets included refer to the effect of valorphins on the size distribution and zeta-potential of POPC LUVs. Investigation of physicochem-ical properties of peptides such as diffusion coefficients and heterogeneous rate constant relates to elucidation of trans-port mechanisms in living cells. Voltammetric data of val-orphins are presented together with square-wave voltammo-grams of investigated peptides for calculation of their hetero-geneous electron transfer rate constants. Datasets from the thermal shape fluctuation analysis of quasispherical 'giant' unilamellar vesicles (GUV) are provided to quantify the in-fluence of hemorphin incorporation on the membrane bend-ing elasticity. Isothermal titration calorimetric data on the thermodynamics of peptide-lipid interactions and the bind-ing affinity of valorphin analogues to phosphatidylcholine membranes are reported. Data of frequency-dependent de-formation of GUVs in alternating electric field are included together with the values of the specific electrical capacitance of POPC-valorphin membranes. The datasets reported in this article can underlie the formulation and implementation of peptide-based strategies in pharmacology and biomedicine.(c) 2022 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license ( http://creativecommons.org/licenses/by/4.0/ )