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.​

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Significance and Impact

Results provide a path for the discovery and optimization of solid-binding peptides for the synthesis of hybrid and programmable materials.

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Research Details

• 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.

Hellner, B., S. Alamdari, H. Pyles, S. Zhang, A. Prakash, K.G. Sprenger, J.J. De Yoreo, D. Baker, J. Pfaendtner, and F. Baneyx. (2020). Sequence-structure-binding relationships reveal adhesion behavior of the Car9 solid-binding peptide: An integrated experimental and simulation study. Journal of the American Chemical Society 142: 2355-2363. DOI: 10.1021/jacs.9b11617

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Work performed at the University of Washington and Pacific Northwest National Laboratory