Modeling binding affinity at peptide-surface interfaces : the role of mutations

While many different peptide sequences have now been experimentally identified to have strong affinity for a huge range of materials, the question of why a given sequence binds so well while another does not remains to be properly answered. Use of molecular simluations is one of many complementary techniques that enables us to address these questions. In this contribution, a summary of our molecular simulation work in this area is presented. We have identified the crucial role of intra-peptide interactions in peptide-inorganic binding for both titania (below) and silica binders. We have also made a detailed investigation of the importance of tryptophan in nanotube-binding peptides via point mutations, and advance a hypothesis based on interfacial shape, explaining why aromatic residues might not dominate in graphite-binding peptides