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...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal Article |
| Language: | English |
| Published: |
2018
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| Online Access: | https://hdl.handle.net/10356/89250 http://hdl.handle.net/10220/46145 |
| _version_ | 1826128966056935424 |
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| author | Petrone, Luigi Kumar, Akshita Sutanto, Clarinda N. Patil, Navinkumar J. Kannan, Srinivasaraghavan Palaniappan, Alagappan Amini, Shahrouz Zappone, Bruno Verma, Chandra Miserez, Ali |
| author2 | School of Materials Science & Engineering |
| author_facet | School of Materials Science & Engineering Petrone, Luigi Kumar, Akshita Sutanto, Clarinda N. Patil, Navinkumar J. Kannan, Srinivasaraghavan Palaniappan, Alagappan Amini, Shahrouz Zappone, Bruno Verma, Chandra Miserez, Ali |
| author_sort | Petrone, Luigi |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T07:33:28Z |
| format | Journal Article |
| id | ntu-10356/89250 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:33:28Z |
| publishDate | 2018 |
| record_format | dspace |
| spelling | ntu-10356/892502023-02-28T17:02:50Z Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins Petrone, Luigi Kumar, Akshita Sutanto, Clarinda N. Patil, Navinkumar J. Kannan, Srinivasaraghavan Palaniappan, Alagappan Amini, Shahrouz Zappone, Bruno Verma, Chandra Miserez, Ali School of Materials Science & Engineering School of Biological Sciences Centre for Biomimetic Sensor Science Biomaterials – Proteins Biophysical Chemistry DRNTU::Engineering::Materials::Biomaterials 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. Published version 2018-10-01T06:32:38Z 2019-12-06T17:21:11Z 2018-10-01T06:32:38Z 2019-12-06T17:21:11Z 2015 Journal Article 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 https://hdl.handle.net/10356/89250 http://hdl.handle.net/10220/46145 10.1038/ncomms9737 26508080 en Nature Communications © 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/ 12 p. application/pdf |
| spellingShingle | Biomaterials – Proteins Biophysical Chemistry DRNTU::Engineering::Materials::Biomaterials Petrone, Luigi Kumar, Akshita Sutanto, Clarinda N. Patil, Navinkumar J. Kannan, Srinivasaraghavan Palaniappan, Alagappan Amini, Shahrouz Zappone, Bruno Verma, Chandra Miserez, Ali Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title | Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title_full | Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title_fullStr | Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title_full_unstemmed | Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title_short | Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins |
| title_sort | mussel adhesion is dictated by time regulated secretion and molecular conformation of mussel adhesive proteins |
| topic | Biomaterials – Proteins Biophysical Chemistry DRNTU::Engineering::Materials::Biomaterials |
| url | https://hdl.handle.net/10356/89250 http://hdl.handle.net/10220/46145 |
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