Evidence map›Paper›PMID 26508080›Full record

ArticleNature communications2015

Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins.

Luigi Petrone, Akshita Kumar, Clarinda N Sutanto, Navinkumar J Patil, Srinivasaraghavan Kannan, Alagappan Palaniappan, Shahrouz Amini, Bruno Zappone, Chandra Verma, Ali Miserez

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed.

  1. Article
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  17. Enzymatic polymerization of enantiomericNature communications · 2023
    Article
  18. Applications of synthetic biology in medical and pharmaceutical fields.Signal transduction and targeted therapy · 2023
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Luigi PetroneSchool of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.ORCID http://orcid.org/0000-0002-3315-3981
Akshita KumarCentre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive, Research Techno Plaza, XFrontiers Block, Singapore 637553, Singapore.
Clarinda N SutantoSchool of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.
Navinkumar J PatilDipartimento di Fisica, Università della Calabria, 87036 Arcavacata di Rende (CS), Italy.
Srinivasaraghavan KannanBioinformatics Institute A*Star, 30 Biopolis Street, Singapore 138671, Singapore.
Alagappan PalaniappanSchool of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.
Shahrouz AminiSchool of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.
Bruno ZapponeConsiglio Nazionale delle Ricerche, CNR-Nanotec, UOS Licryl-Cosenza, 87036 Rende (CS), Italy.
Chandra VermaSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
Ali MiserezSchool of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore 639798, Singapore.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsBivalviaMolecular Dynamics SimulationProtein ConformationProteinsProtein TransportSecretory PathwayTime Factorsadhesive protein, musselProteins

Identifiers

PMID26508080
PMCPMC4640085

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.