Insights into the behavior of six rationally designed peptides based on Escherichia coli's OmpA at the water-dodecane interface release_gjjbi5uem5h3pnhr2ma33rhzym

by Miguel Fernández-Niño, Lina Rojas, Javier Cifuentes, Rodrigo Torres, Andrea Ordoñez, Juan C. Cruz, Edgar Francisco Vargas, Diego Pradilla, Oscar Álvarez Solano, Andrés González Barrios

Published in PLoS ONE by Public Library of Science (PLoS).

2019   Volume 14, Issue 10, e0223670


The Escherichia coli's membrane protein OmpA has been identified as a potential biosurfactant due to their amphiphilic nature, and their capacity to stabilize emulsions of dodecane in water. In this study, the influence of surfactant type, concentration, preservation time and droplet size on the crystallization of n-dodecane and water, in oil-in-water emulsions stabilized with six rationally designed Escherichia coli's OmpA-based peptides was investigated. A differential scanning calorimetry (DSC) protocol was established using emulsions stabilized with Tween 20® and Tween 80®. A relationship between the surfactant concentration and the crystallization temperatures of n-dodecane and water was observed, where the crystallization temperatures seem to be dependent on the preservation time. A deconvolution analysis shows that the peak morphology possibly depends on the interactions at the interface because the enthalpic contributions of each Gaussian peak remained similar in emulsions stabilized with the same peptide. Adsorption results show that the main driver for adsorption and thus stabilization of emulsions is polar interactions (e.g. H-bonding) through the hydrophilic parts of the peptides. Those peptides with a preponderance of polar interaction groups distribution (i.e. NH2, COOH, imidazole) showed the highest interfacial activity under favorable pH conditions. This suggests that custom-made peptides whose hydrophilic/hydrophobic regions can be fine-tuned depending on the application can be easily produced with the additional advantage of their biodegradable nature.
In text/plain format

Archived Files and Locations

application/pdf  2.1 MB
file_4cbk2dhsxfbp5dxcjiv3kt2fwu (aggregator) (publisher) (webarchive) (webarchive)
Read Archived PDF
Type  article-journal
Stage   published
Date   2019-10-10
Language   en ?
Container Metadata
Open Access Publication
Not in Keepers Registry
ISSN-L:  1932-6203
Work Entity
access all versions, variants, and formats of this works (eg, pre-prints)
Catalog Record
Revision: ecf190d5-7620-4cd1-a5bc-61febf6f17e4