Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncomms9737
Title: Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Authors: Petrone, L
Kumar, A
Sutanto, C.N
Patil, N.J
Kannan, S
Palaniappan, A
Amini, S
Zappone, B
Verma, C 
Miserez, A
Keywords: adhesion
homology
interface
molecular analysis
mollusc
protein
secretion
Musculista senhousia
Perna viridis
adhesive protein, mussel
protein
animal
bivalve
chemistry
genetics
metabolism
molecular dynamics
physiology
protein conformation
protein transport
secretory pathway
time factor
Animals
Bivalvia
Molecular Dynamics Simulation
Protein Conformation
Protein Transport
Proteins
Secretory Pathway
Time Factors
Issue Date: 2015
Publisher: Nature Publishing Group
Citation: Petrone, L, Kumar, A, Sutanto, C.N, Patil, N.J, Kannan, S, Palaniappan, A, Amini, S, Zappone, B, Verma, C, Miserez, A (2015). Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins. Nature Communications 6 : 8737. ScholarBank@NUS Repository. https://doi.org/10.1038/ncomms9737
Rights: Attribution 4.0 International
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. © 2015 Macmillan Publishers Limited. All rights reserved.
Source Title: Nature Communications
URI: https://scholarbank.nus.edu.sg/handle/10635/180421
ISSN: 2041-1723
DOI: 10.1038/ncomms9737
Rights: Attribution 4.0 International
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