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.
Scientific Achievement
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.
Research Details
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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.
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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.
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AFM confirmed predictions and SPR measurements.