Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins

Luigi Petrone, Akshita Kumar, Clarinda N. Sutanto, Navinkumar J. Patil, Srinivasaraghavan Kannan, Alagappan Palaniappan, Shahrouz Amini, Bruno Zappone, Chandra Verma and Ali Miserez ()
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Luigi Petrone: School of Materials Science and Engineering, Nanyang Technological University
Akshita Kumar: Centre for Biomimetic Sensor Science, Nanyang Technological University
Clarinda N. Sutanto: School of Materials Science and Engineering, Nanyang Technological University
Navinkumar J. Patil: Università della Calabria
Srinivasaraghavan Kannan: Bioinformatics Institute A*Star
Alagappan Palaniappan: School of Materials Science and Engineering, Nanyang Technological University
Shahrouz Amini: School of Materials Science and Engineering, Nanyang Technological University
Bruno Zappone: Consiglio Nazionale delle Ricerche, CNR-Nanotec, UOS Licryl-Cosenza
Chandra Verma: School of Biological Sciences, Nanyang Technological University
Ali Miserez: School of Materials Science and Engineering, Nanyang Technological University

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract Interfacial water constitutes a formidable barrier to strong surface bonding, hampering the development of water-resistant synthetic adhesives. Notwithstanding this obstacle, the Asian green mussel Perna viridis attaches firmly to underwater surfaces via a proteinaceous secretion (byssus). Extending beyond the currently known design principles of mussel adhesion, here we elucidate the precise time-regulated secretion of P. viridis mussel adhesive proteins. The vanguard 3,4-dihydroxy-L-phenylalanine (Dopa)-rich protein Pvfp-5 acts as an adhesive primer, overcoming repulsive hydration forces by displacing surface-bound water and generating strong surface adhesion. Using homology modelling and molecular dynamics simulations, we find that all mussel adhesive proteins are largely unordered, with Pvfp-5 adopting a disordered structure and elongated conformation whereby all Dopa residues reside on the protein surface. Time-regulated secretion and structural disorder of mussel adhesive proteins appear essential for optimizing extended nonspecific surface interactions and byssus’ assembly. Our findings reveal molecular-scale principles to help the development of wet-resistant adhesives.

Date: 2015
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DOI: 10.1038/ncomms9737

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