Towards rational de novo design of peptides for inorganic interfaces

Abstract

Proteins at inorganic interfaces occur across science, technology and nature – protein arrays, prostheses such as stents and artificial heart valves, biomimetic assembly of nanoparticles, and anti-freeze proteins are just a few examples from many. Despite the clear importance of proteins at inorganic interfaces, elucidation of the structure and behaviour of proteins at such interfaces and the design of associated systems is still dominated by experiment, and trial and error. We at Edinburgh are developing computational tools that will complement this experimental effort. In this presentation, I will outline the overall approach we are seeking to develop for the rational de novo design of systems involving proteins at solid interfaces – which exploits in silico evolutionary processes – and then provide details (with examples) of the various elements involved. As part of this, I will present results for the ab initio prediction of protein conformations in the gas and liquid phases and at solid surfaces, and a molecular switching phenomenon we have observed in polyalanine that may be of relevance to nanotechnology and disease processes.