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

Nature Communications2015Vol. 6(1), pp. 8737–8737

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Luigi Petrone, Akshita Kumar, Clarinda Nataria Sutanto, Navinkumar J. Patil, Srinivasaraghavan Kannan, Alagappan Palaniappan, Shahrouz Amini, Bruno Zappone, Chandra Verma, Ali Miserez

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.

Citations Over TimeTop 10% of 2015 papers

Abstract

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