Subject	Materials Science
Specific subject area	Soft matter characterization; biomimetic self-assembling molecules; synthetic opioid peptides; liposomal formulations; lipid membrane deformability
Type of data	Tables and Figures
How the data were acquired	Data on VV-hemorphin-5 interactions with lipid membranes refer to bilayer lipid models produced by electroformation of giant unilamellar quasispherical lipid vesicles and extrusion of large unilamellar lipid vesicles (LiposoFast, Avestin, Ottawa, Canada). The peptides investigated herein were obtained by solid phase synthesis [1]. Bending elasticity data were acquired by means of phase-contract light microscopy (Axiovert 100, Zeiss, Germany) and analysis of thermal shape fluctuations (ATSF) of giant unilamellar quasispherical lipid vesicles [2]. Specific electrical capacitance data of POPC-valorphin membranes were obtained from frequency-dependent electrodeformation (ED) data
	of GUVs in alternating electric field [3]. Square-wave cyclic voltammetry (Metrohm 797, Switzerland; Pt and Ag/AgCl electrodes) was applied to evaluate the heterogeneous electron transfer rate constants of peptides [4]. Isothermal titration calorimetry in multiple injection mode (NanoITC calorimeter, TA Instruments, Lindon, UT, USA) provided the heat of LUV dilution in hemorphin solutions, and the peptide-lipid binding isotherms. Dynamic light scattering and laser Doppler electrophoresis of large unilamellar vesicles were acquired by Zetasizer Advance Series Instrument (Malvern Analytical, United Kingdom) with a 4 mW 632.8 nm sample illumination and detection at 173°. Fluorescence spectroscopy data of dye-labelled membranes (FP-8300, Jasco, MD, USA) refer to Laurdan spectra recorded from 390 to 600 nm upon excitation at 355 nm, and to di-8-ANEPPS fluorescence intensity ratio at 670 nm upon excitation at 420 nm and 520 nm [5].
Data format	Raw Data Analyzed Data
Description of data collection	The values of the bending modulus reported in the present article were calculated from ATSF data on populations of 6 to 13 GUVs accepted according to algorithms applied for elimination of systematic artifacts including correlated contours, volume and surface changes, non-quasisphericity, blurred contours, and membrane defects [2]. Fluorescence spectroscopy data were collected from 20 measurements of two different LUV preparations for each peptide investigated. Membrane capacitance values were reported based on the electrodeformation data of 9 to 30 GUVs. Prior to evaluation of reaction enthalpies and binding isotherms ITC data were corrected by the average area of dilution peaks [6]. Electrochemical data are reported as the mean value of three independent measurements. Data on average vesicle sizes were calculated from multi-angle dynamic light scattering signal acquired from six independent measurements. The same number of runs was performed to obtain the electrophoretic mobility datasets.
Data source location	Institute of Solid State Physics, Bulgarian Academy of Sciences, 72, Tzarigradsko Chaussee, Blvd, 1784 Sofia, Bulgaria 42°39′09.5″N 23°23′18.6″E
Data accessibility	Available with this article and also at: https://data.mendeley.com/datasets/gs6wxvcvs6/2
Related research article	V. Vitkova, G. Staneva, R. Hazarosova, St. Georgieva, I. Valkova, K. Antonova, P. Todorov, Interaction of new VV-hemorphin-5 analogues with cell membrane models, Coll. Surf. B, 220 (2022) 112896 https://doi.org/10.1016/j.colsurfb.2022.112896