Adhesive properties of adsorbed layers of two recombinant mussel foot proteins with different levels of DOPA and tyrosine.

Clicks: 252
ID: 24300
2019
Article Quality & Performance Metrics
Overall Quality
Not rated
Combines reader engagement with the AI quality analysis. This article has not been analysed, so there is no overall score — reader engagement is measured and shown alongside.
AI Quality Assessment
Not analyzed
Readership in this journal
Steady

Ranked #46 of 87 articles by views in Langmuir : the ACS journal of surfaces and colloids

Most read Least read

Bar heights use a square-root scale.

Mint this article as an NFT
Not yet minted

Create a permanent, verifiable on-chain record of this article on the Scimatic Network. The NFT is held in your Journament account, and you can withdraw it to your own wallet at any time.

5 SUSD one-off · no wallet required
Sign in to mint
Abstract
Using a Surface Forces Apparatus and an Atomic Force Microscope, we characterized the adhesive properties of adsorbed layers of two recombinant variants of foot protein 5 (PVFP-5), the main surface-binding protein in the adhesive plaque of the Asian green mussel. In one variant, all tyrosine residues were modified into 3,4-dihydroxy-L-phenylalanine (DOPA) during expression using a residue-specific incorporation strategy. DOPA is a key molecular moiety underlying underwater mussel adhesion. In the other variant, all tyrosine residues were preserved. The layer was adsorbed on a mica substrate and pressed against an uncoated surface. While DOPA produced a stronger adhesion than tyrosine in contact with the nanoscopic SiN probe of the Atomic Force Microscope, the two variants produced comparable adhesion with curved macroscopic mica surfaces in the Surface Forces Apparatus. These findings show that the presence of DOPA is not a sufficient condition to generate strong underwater adhesion. Surface chemistry and contact geometry affect the strength and abundance of protein-surface bonds created during adsorption and surface contact. Importantly, the adsorbed protein layer has a random and dynamic polymer-network structure that should be optimized to transmit the tensile stress generated during surface separation to DOPA surface bonds rather than other weaker bonds.
Reference Key
bilotto2019adhesivelangmuir Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Bilotto, Pierluigi;Labate, Cristina;De Santo, Maria Penelope;Deepankumar, Kanagavel;Miserez, Ali;Zappone, Bruno;
Journal Langmuir : the ACS journal of surfaces and colloids
Year 2019
DOI
10.1021/acs.langmuir.9b01730
URL
Keywords Keywords not found

Citations

No citations found. To add a citation, contact the admin at info@scimatic.org

Comments

No comments yet. Be the first to comment on this article.