Abstract
Engineering peptides that present selective recognition and high affinity towards a material is a major challenge for assembly-driven elaboration of complex systems with wide applications in the field of biomaterials, hard-tissue regeneration and functional materials for therapeutics. Peptide–material interactions are of vital importance in natural processes, but less exploited for the design of novel systems for practical applications due to poor understanding of mechanisms underlying these interactions. Here, we present an approach based on the synthesis of several truncated peptides issued from a silicon-specific peptide recovered via phage display technology. We use the photonic response provided by porous silicon microcavities to evaluate the binding efficiency of fourteen different peptide derivatives. We identify and engineer a short peptide sequence (SLVSHMQT) revealing the highest affinity towards p+ -Si. The molecular recognition behavior of the obtained peptide fragment can be revealed through mutations enabling identification of the preferential affinity of certain amino acids towards silicon. These results constitute an advance in both the engineering of peptides that reveal recognition properties for silicon and the understanding of biomolecule-material interactions.