Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.
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.
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.|Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
Luigi
http://orcid.org/0000-0002-3315-3981
L
Petrone
Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.|School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
Akshita
A
Kumar
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.|Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
Clarinda N
CN
Sutanto
Dipartimento di Fisica, Università della Calabria, 87036 Arcavacata di Rende (CS), Italy.
Navinkumar J
NJ
Patil
Bioinformatics Institute A*Star, 30 Biopolis Street, Singapore 138671, Singapore.
Srinivasaraghavan
S
Kannan
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.|Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
Alagappan
A
Palaniappan
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.|Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
Shahrouz
S
Amini
Consiglio Nazionale delle Ricerche, CNR-Nanotec, UOS Licryl-Cosenza, 87036 Rende (CS), Italy.
Bruno
B
Zappone
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.|Bioinformatics Institute A*Star, 30 Biopolis Street, Singapore 138671, Singapore.|Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.
Chandra
C
Verma
School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.|Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.|School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
Ali
A
Miserez
D000818:Animals; D049872:Bivalvia / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055571:Secretory Pathway; D013997:Time Factors
D011506:Proteins; C037403:adhesive protein, mussel