Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/89250
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dc.contributor.authorPetrone, Luigien
dc.contributor.authorKumar, Akshitaen
dc.contributor.authorSutanto, Clarinda N.en
dc.contributor.authorPatil, Navinkumar J.en
dc.contributor.authorKannan, Srinivasaraghavanen
dc.contributor.authorPalaniappan, Alagappanen
dc.contributor.authorAmini, Shahrouzen
dc.contributor.authorZappone, Brunoen
dc.contributor.authorVerma, Chandraen
dc.contributor.authorMiserez, Alien
dc.date.accessioned2018-10-01T06:32:38Zen
dc.date.accessioned2019-12-06T17:21:11Z-
dc.date.available2018-10-01T06:32:38Zen
dc.date.available2019-12-06T17:21:11Z-
dc.date.issued2015en
dc.identifier.citationPetrone, 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/ncomms9737en
dc.identifier.urihttps://hdl.handle.net/10356/89250-
dc.description.abstractInterfacial 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.en
dc.format.extent12 p.en
dc.language.isoenen
dc.relation.ispartofseriesNature Communicationsen
dc.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/en
dc.subjectBiomaterials – Proteinsen
dc.subjectBiophysical Chemistryen
dc.subjectDRNTU::Engineering::Materials::Biomaterialsen
dc.titleMussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteinsen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Materials Science & Engineeringen
dc.contributor.schoolSchool of Biological Sciencesen
dc.contributor.researchCentre for Biomimetic Sensor Scienceen
dc.identifier.doi10.1038/ncomms9737en
dc.description.versionPublished versionen
item.grantfulltextopen-
item.fulltextWith Fulltext-
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