Tailor Designed Peptides Bio-Inspired from Transmembrane Proteins for the Cosmetic Industry

Surfactants are amphiphilic compounds with the ability to radically alter surface and interfacial properties. These properties are highly desired in food, health, personal care, and oil industries in which there are several processes related with stabilization of emulsions. Several efforts have been invested on the search of environmentally benign products, and there is a need for a strategy to identify biosurfactants that can replace conventional ones. The aim of this work is to evaluate transmembrane protein-engineered peptides via Free Energy (FE) Molecular Dynamics (MD) and to compare them against the already experimentally tested OmpA₃₂₅. Sixteen protein-engineered peptides were selected from the sequence of OmpA₃₂₅ as potential biosurfactants based on its hydrophobic profile. The FE-methodology comprised a series of MD simulations of the path between two states of interest, discretized by several intermediate ones, and coupling van der Waals and Coulomb interactions separately. After FE-MD, an analysis from the simulations to obtain a statistical estimate for the free energy with the Bennett’s acceptance ratio (BAR) method was performed. Analysis of the 5-ns MD trajectories showed the potential ability of all peptides to increase the system’s stability. Negative ΔG_solv was achieved in all cases, with significant phase-space overlap and nearly-zero standard deviations. Then they were scored and ranked by taking into account the ΔG_solv, solvent accessible surface area (SASA), molecular weight (MW), and ΔG_Coul/ΔG_vdW ratio for final experimental validation utilizing water-dodecane emulsions with each synthetized peptided  where stability and drop size distribution were evaluated and compared with the list provided by MD simulations.