Abstract
As a group membrane proteins (such as OmpA, a membrane protein of mainly Gram-negative bacteria) has emerged  as an active area of research since the proteins have a natural role in biological processes. Most of the research interest centers on their amphiphilic nature; specifically with regard to OmpA, the capacity to stabilize emulsions of dodecane in water has exciting and widespread implications. However, little is known about a membrane protein’s mode of attracting water and lipophilic molecules. Here, we have focused on the surface activity of two membrane proteins of Escherichia coli (OmpA and OmpN) in order to compare their emulsifier capacity within a media composed of water and triglycerides. For this, we have employed a molecular dynamics strategy, evaluating variables such as the unsaturation pattern and the fatty acid chain length on the triglyceride molecule. A direct relation with the protein solvent accessible surface area and the unsaturation pattern of the lipid molecules has been observed. Additionally, the radius of gyration has been identified as an indicator of the protein’s capacity to relax its secondary structure to enhance its surfactant activity. The presentation will also discuss the use of Agent Based Modeling as a multiscale modeling platform that allows the bridging of length and time scales when dealing with larger protein biosurfactants.

On the use of molecular dynamics in the simulation of outer membrane proteins which act as biosurfactants in triglycerides/water emulsions

ACS Fall 2020 Virtual Meeting

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