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Vibrio cholerae adhesin-derived peptide mediates strong pull-off forces in aqueous high-ionic-strength environments
Syeda Tajin Ahmed1, Sixin Zhai2, Xin Huang3
1Department of Chemical and Materials Engineering, University of California, Merced, Merced, CA 94344, USA.
Biorxiv : the Preprint Server for Biology
|September 5, 2025
Summary
This study investigated Bap1-inspired peptide adhesion on mica, finding that hydrophobic peptides exhibit strong pull-off forces, especially with salt. Salt also promotes peptide aggregation, influencing film thickness.
Area of Science:
- Biomaterials Science
- Surface Chemistry
- Peptide Engineering
Background:
- Understanding peptide-surface interactions is crucial for biomaterial design.
- Bap1 peptides inspire novel adhesive materials.
- Mussel foot proteins serve as a benchmark for bio-inspired adhesion.
Purpose of the Study:
- To measure the pull-off forces of Bap1-inspired peptides on mica.
- To investigate the influence of solvents and salt on peptide adhesion.
- To correlate solution aggregation behavior with film properties.
Main Methods:
- Surface Forces Apparatus (SFA) for measuring adhesion forces.
- Dynamic Light Scattering (DLS) for characterizing peptide aggregation.
- Utilized four Bap1-inspired peptide variants (WT, Scr, CP, Sh1).
Main Results:
- The hydrophobic CP peptide showed significant pull-off forces (up to 42.0 mN/m with salt and dwell time).
- Salts induced large peptide aggregation (>1 µm) across all constructs.
- Peptide aggregation led to heterogeneous film thicknesses.
Conclusions:
- Hydrophobic interactions and salt concentration significantly enhance peptide adhesion.
- Peptide aggregation in solution directly impacts the structure and adhesion of adsorbed films.
- Bap1-inspired peptides show promise for adhesive applications, comparable to mussel foot proteins.
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