Author
Listed:
- Luigi Petrone
(School of Materials Science and Engineering, Nanyang Technological University
Centre for Biomimetic Sensor Science, Nanyang Technological University)
- Akshita Kumar
(Centre for Biomimetic Sensor Science, Nanyang Technological University
School of Biological Sciences, Nanyang Technological University)
- Clarinda N. Sutanto
(School of Materials Science and Engineering, Nanyang Technological University
Centre for Biomimetic Sensor Science, Nanyang Technological University)
- Navinkumar J. Patil
(Università della Calabria)
- Srinivasaraghavan Kannan
(Bioinformatics Institute A*Star)
- Alagappan Palaniappan
(School of Materials Science and Engineering, Nanyang Technological University
Centre for Biomimetic Sensor Science, Nanyang Technological University)
- Shahrouz Amini
(School of Materials Science and Engineering, Nanyang Technological University
Centre for Biomimetic Sensor Science, Nanyang Technological University)
- Bruno Zappone
(Consiglio Nazionale delle Ricerche, CNR-Nanotec, UOS Licryl-Cosenza)
- Chandra Verma
(School of Biological Sciences, Nanyang Technological University
Bioinformatics Institute A*Star
National University of Singapore)
- Ali Miserez
(School of Materials Science and Engineering, Nanyang Technological University
Centre for Biomimetic Sensor Science, Nanyang Technological University
School of Biological Sciences, Nanyang Technological University)
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.
Suggested Citation
Luigi Petrone & Akshita Kumar & Clarinda N. Sutanto & Navinkumar J. Patil & Srinivasaraghavan Kannan & Alagappan Palaniappan & Shahrouz Amini & Bruno Zappone & Chandra Verma & Ali Miserez, 2015.
"Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins,"
Nature Communications, Nature, vol. 6(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9737
DOI: 10.1038/ncomms9737
Download full text from publisher
Citations
Citations are extracted by the
CitEc Project, subscribe to its
RSS feed for this item.
Cited by:
- Yuhe Shen & Rongxin Su & Dongzhao Hao & Xiaojian Xu & Meital Reches & Jiwei Min & Heng Chang & Tao Yu & Qing Li & Xiaoyu Zhang & Yuefei Wang & Yuefei Wang & Wei Qi, 2023.
"Enzymatic polymerization of enantiomeric L−3,4-dihydroxyphenylalanine into films with enhanced rigidity and stability,"
Nature Communications, Nature, vol. 14(1), pages 1-13, December.
- Yongchun Liu & Ke Li & Juanhua Tian & Aiting Gao & Lihua Tian & Hao Su & Shuting Miao & Fei Tao & Hao Ren & Qingmin Yang & Jing Cao & Peng Yang, 2023.
"Synthesis of robust underwater glues from common proteins via unfolding-aggregating strategy,"
Nature Communications, Nature, vol. 14(1), pages 1-15, December.
- Qi Guo & Guijin Zou & Xuliang Qian & Shujun Chen & Huajian Gao & Jing Yu, 2022.
"Hydrogen-bonds mediate liquid-liquid phase separation of mussel derived adhesive peptides,"
Nature Communications, Nature, vol. 13(1), pages 1-10, December.
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9737. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.