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| Content Provider | PubMed Central |
|---|---|
| Author | Petrone, Luigi Kumar, Akshita Sutanto, Clarinda N. Patil, Navinkumar J. Kannan, Srinivasaraghavan Palaniappan, Alagappan Amini, Shahrouz Zappone, Bruno Verma, Chandra Ali, Miserez |
| Copyright Year | 2015 |
| 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. |
| Related Links | http://dx.doi.org/10.1038/ncomms9737 |
| Starting Page | 8737 |
| File Format | |
| ISSN | 20411723 |
| e-ISSN | 20411723 |
| Journal | Nature Communications |
| Volume Number | 6 |
| Language | English |
| Publisher | Nature Pub. Group |
| Publisher Date | 2015-10-28 |
| Access Restriction | Open |
| Rights Holder | Nature Pub. Group |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry Physics and Astronomy Biochemistry, Genetics and Molecular Biology |
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