Analysis of peptide - gold (Au) {111}-surface interactions

Proteins are known to have a role in mineral nucleation, growth, and structure creation, as well as providing molecular scaffolding for the formation of soft and hard tissues such as bone and dental tissues. Today in bionanotechnology, proteins and peptides are used in various fields such as biosynthesis, biosensors, drug delivery and targeting, integrated with inorganic materials (Ag, SiO2, TiO2, Pd, Pt, graphene, hydroxyapatite, etc.). Here, specific binding of peptides to materials affects device performance and this specifity is related to peptide sequences and structures. Today, these peptides are selected with inspration from nature or combinatorial selection methods. So, a deeper understanding of interactions between inorganic materials and peptides/proteins and design of peptides with desired specifity and properties is very important for the improvement of technology. Gold is a highly conductive inorganic and amenable to surface modifications. When gold is functionalized with peptides, it has practical applications such as bioimaging, biosensors, cancer therapy and drug delivery. In this research, we use atomistic methods (NAMD) to understand how peptides interact with Au {111}-surface. In this study, the binding mechanisms of well known peptides that binds to Au {111}-surface are found out. In addition, two peptides are designed via optimization of peptide sequences, binding structures and affinities to Au {111}-surface.