Conformations of myoglobin-derived peptides at the air-water interface

Abstract

The conformational change exhibited by proteins at liquid interfaces, such as the air-water and oil-water interfaces, has long been of interest, both for understanding protein structure outside of native environments and for applications in areas including food technology and pharmaceuticals. Using molecular simulation this paper studies the conformations of two peptides derived from myoglobin, for which the emulsification behaviour has been studied. Both peptides were found to readily adsorb onto the air-water interface, with one of these (experimentally the more effective stabiliser) adopting a flat, extended conformation, with the other peptide remaining close its solution conformation.