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Sequence-Structure-Binding Relationships Reveal Adhesion Behavior of the Car9 Solid-Binding Peptide: An Integrated
Brittney Hellner, Sarah Alamdari, Harley Pyles
1Physical Sciences Division, Physical and Computational Sciences Directorate , Pacific Northwest National Laboratory , Richland , Washington 99352 , United States.
Journal of the American Chemical Society
|January 15, 2020
Summary
Solid-binding peptides (SBPs) can adhere to surfaces, but how they interact remains unclear. This study reveals that electrostatic forces and peptide self-association drive strong binding, enabling new materials design.
Area of Science:
- Materials Science
- Biotechnology
- Protein Engineering
Background:
- Solid-binding peptides (SBPs) are crucial for materials science applications, acting as genetic linkers for protein frameworks.
- Understanding SBP-surface and SBP-SBP interactions is key to controlling adsorption mechanisms.
Purpose of the Study:
- To investigate the relationships between amino acid composition, structure, self-association, and adhesion in Car9 silica-binding peptide variants.
- To elucidate the mechanisms governing SBP adhesion to silica surfaces.
Main Methods:
- Protein engineering of superfolder green fluorescent protein (sfGFP)-Car9 variants.
- Surface plasmon resonance (SPR) for kinetic and energetic analysis.
- Molecular dynamics (MD) simulations initiated from Rosetta predictions.
- Atomic force microscopy (AFM) for imaging binding behaviors.
Main Results:
- High-affinity Car9 binding to silica is driven by electrostatics and persistent interactions, promoting SBP self-association and higher-order structures.
- A transition from cooperative to Langmuir adhesion was observed with reduced SBP self-association.
- AFM confirmed distinct binding behaviors corresponding to cooperative and Langmuir adhesion.
Conclusions:
- Electrostatic interactions and SBP self-association are critical for strong, cooperative binding to silica.
- Modulating these interactions allows control over adhesion mechanisms, transitioning from cooperative to Langmuir binding.
- Findings provide insights for the rational design of novel SBP-surface binding systems.
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