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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Petrone L,Kumar A,Sutanto CN,Patil NJ,Kannan S,Palaniappan A,Amini S,Zappone B,Verma C,Miserez A

doi

10.1038/ncomms9737

subject

Has Abstract

pub_date

2015-10-28 00:00:00

pages

8737

issn

2041-1723

pii

ncomms9737

journal_volume

6

pub_type

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