Uncovering Relationships between Peptide Sequence, Structure, and Inorganic Adhesion Behavior
January 14, 2020
Silica-bound structures of wild type and mutant Car9 peptides predicted by MD simulations initiated from Rosetta calculations lead to self-association (P9AG10A) or not (K8K11A). This results in either cooperative or Langmuir binding.
Deep integration of simulations and experiments explains how the amino acid sequence of a silica-binding peptide determines its interfacial configuration, self-association, and adhesion behavior.
Significance and Impact
Results provide a path for the discovery and optimization of solid-binding peptides for the synthesis of hybrid and programmable materials.
The binding kinetics of a panel of mutants of the Car9 silica-binding peptide fused to green fluorescent protein were acquired by SPR and modeled to correlate rate constants and free energies with adhesion modality.
Molecular dynamics simulations on silica initiated from solution Rosetta calculations provided information on anchor residues, peptide conformational flexibility, and propensity to oligomerize at the SiO₂ interface.
AFM confirmed predictions and SPR measurements.