MD Simulations of Sequence Tuned Peptides Supramolecular Structures on Graphene Interface

Abstract

Peptide conformations are pivotal for biomolecular interactions that determine to a great deal biofunctional activities. State-of-the-art experiments provide limited insight into molecular scale aspects of the weak interactions of these soft and complex macromolecules. This molecular dynamic simulation project utilizes microscopic data of directed evolution selected solid binding peptides to provide a fundamental understanding of the relationship between sequence, peptide structure and interfacial assembly on inorganic surfaces, such as graphene. Specifically, we use enhanced sampling computational methodologies to identify dominant structures of two peptides with similar sequence. With these dominant structures, we can identify the most stable peptide conformations on the mentioned inorganic substrate surfaces with relative orientational relationships and interactions that provide us with the necessary input to predict the patterning structure of single peptide phases, as well as immiscible phase mixtures.