The integration of computational and experimental approaches to understand complex biological systems is an emerging research paradigm. Using this approach, we have studied the structures and functions of a 20-mer peptide P1ASP1 in different environments. Initial structures of the peptide were predicted uisng ROSETTA. Using AMBER99SB forcefield, the lowest energy conformation (hairpin-like structure) of the peptide was obtained from replica exchange molecular dynamics simulations. The structures and functions of P1ASP1 adsorbed on carbon nanomaterials were then investigated uisng atomic-scale molecular dynamics simulations. Upon adsorption onto a single-wall carbon nanotube (SWCNT), the hairpin structure is retained. One beta strand lays on the surface, while the other beta strand enables the peptide to capture a target molecule. Conversely, when the peptide is adsorbed onto a flat graphene sheet, it becomes disordered and loses its binding affinity. Corresponding experimental studies included CD spectroscopy, AFM images and SWCNT/graphene FET-based sensing experiments.

Adsorption-induced conformational and functional changes of a peptide on carbon nanostructures

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.