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Nat Commun. 2015 Oct 28;6:8737. doi: 10.1038/ncomms9737.

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

Author information

1
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.
2
Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
3
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
4
Dipartimento di Fisica, Università della Calabria, 87036 Arcavacata di Rende (CS), Italy.
5
Bioinformatics Institute A*Star, 30 Biopolis Street, Singapore 138671, Singapore.
6
Consiglio Nazionale delle Ricerche, CNR-Nanotec, UOS Licryl-Cosenza, 87036 Rende (CS), Italy.
7
Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.

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.

PMID:
26508080
PMCID:
PMC4640085
DOI:
10.1038/ncomms9737
[Indexed for MEDLINE]
Free PMC Article

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