Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89250
Title: Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Authors: Petrone, Luigi
Kumar, Akshita
Sutanto, Clarinda N.
Patil, Navinkumar J.
Kannan, Srinivasaraghavan
Palaniappan, Alagappan
Amini, Shahrouz
Zappone, Bruno
Verma, Chandra
Miserez, Ali
Keywords: Biomaterials – Proteins
Biophysical Chemistry
DRNTU::Engineering::Materials::Biomaterials
Issue Date: 2015
Source: Petrone, L., Kumar, A., Sutanto, C. N., Patil, N. J., Kannan, S., Palaniappan, A., . . . Miserez, A. (2015). Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins. Nature Communications, 6, 8737-. doi:10.1038/ncomms9737
Series/Report no.: Nature Communications
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.
URI: https://hdl.handle.net/10356/89250
http://hdl.handle.net/10220/46145
DOI: http://dx.doi.org/10.1038/ncomms9737
Rights: © 2015 Macmillan Publishers Limited. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
metadata.item.grantfulltext: open
metadata.item.fulltext: With Fulltext
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