Surface defect sites facilitate fibrillation: an insight into adsorption of gold-binding peptides on Au(111)

Abstract

We report new evidence on the surface defect dependent fibrillation of cysteine-free gold-binding peptides (identified from a phage-display peptide library) upon adsorption onto the Au(111) surface revealed using atomic force microscopy (AFM). Dramatic changes in the persistence length and binding conformation of the peptide fibrils on Au(111) have been demonstrated to occur via surface reorganization of the peptide. Moreover, surface defect sites played a governing role in initiating fibrillation. These observations could provide new insight into engineering bio–nano interfaces for self-assembly, biotemplating and biotic–abiotic hybrid material systems and device platforms.