Uncovering mussel foot protein (Mfp-3)'s binding secrets: Enhanced biomimetic adhesives via mass spectrometry and residue labeling

This study delves into the development of biomimetic adhesives, taking inspiration from the impressive underwater adhesion of mussels. In a departure from the traditional focus on DOPA, we explore a more comprehensive range of amino acids crucial for adhesion in wet environments. By utilizing amino...

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Bibliographic Details
Published in:Colloids and surfaces. A, Physicochemical and engineering aspects Physicochemical and engineering aspects, 2024-12, Vol.702, p.134953, Article 134953
Main Authors: Liu, Yu-Syuan, Li, Yiran, Su, Wen-Yu, Jian, Ting-Han, Kao, Chuan-Tse, Tsai, Yu-Yu, Tsai, Chia-Ju, Thyparambil, Aby, Wei, Yang
Format: Article
Language:English
Subjects:
Amino acid residue labeling
Binding sequence
Bioinspired adhesive
Mass spectrometry
Mussel foot proteins
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Summary:This study delves into the development of biomimetic adhesives, taking inspiration from the impressive underwater adhesion of mussels. In a departure from the traditional focus on DOPA, we explore a more comprehensive range of amino acids crucial for adhesion in wet environments. By utilizing amino acid labeling and mass spectrometry-based peptide mapping, we identify key peptide sequences within Mfp-3 responsible for effective aquatic adhesion. Of particular interest is the sequence YNRYARGY, which exhibits robust adhesion on both polar/acidic and hydrophobic surfaces, with an adsorption-free energy of approximately -4.5 kcal/mol (as determined by QCM). Incorporating this sequence (1% w/v), with tyrosine substitution for DOPA, into a standard PVA binder significantly enhances its adhesion capabilities. Lap-shear tests demonstrate a significant increase in PVA adhesion from 2.5 to 5 kPa on SiO2 and from 2.1 to 3.3 kPa on HDPE. These findings highlight the practical implications of our mass spectrometry approach with side chain modification in elucidating the mechanisms of mussel adhesion, thereby offering a promising strategy for advancing polymer adhesion technology. [Display omitted] •Mfp-3 holds bioadhesive promise amid yield challenges.•Amino acid labeling and mass spectrometry unveil Mfp-3's adhesive sequence.•Secondary bonding and structural adaptation amplify adsorption strength.•Improved adhesion of PVA by blending with peptide on HDPE and SiO2 surfaces.
ISSN:0927-7757
DOI:10.1016/j.colsurfa.2024.134953