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

• Main Authors: Petrone, Luigi, Kumar, Akshita, Sutanto, Clarinda N., Patil, Navinkumar J., Kannan, Srinivasaraghavan, Palaniappan, Alagappan, Amini, Shahrouz, Zappone, Bruno, Verma, Chandra, Miserez, Ali
• Other Authors: School of Materials Science & Engineering
• Format: Article
• Language: English
• Published: 2018
• Subjects: Biomaterials – Proteins; Biophysical Chemistry; DRNTU::Engineering::Materials::Biomaterials
• Online Access: https://hdl.handle.net/10356/89250; http://hdl.handle.net/10220/46145
• Institution: Nanyang Technological University

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.