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

Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Title:
Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Other Titles:
Nature Communications
Keywords:
Publication Date:
28 October 2015
Citation:
Nature Communications volume 6, Article number: 8737 (2015) doi:10.1038/ncomms9737
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.
License type:
http://creativecommons.org/licenses/by/4.0/
Funding Info:
Description:
ISSN:
2041-1723
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