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Protein Adsorption on Materials and Its Applications

A special issue of Materials (ISSN 1996-1944). This special issue belongs to the section "Biomaterials".

Deadline for manuscript submissions: closed (30 June 2021) | Viewed by 2945

Special Issue Editor


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Guest Editor
European Institute of Membranes, University of Montpellier, 34095 Montpellier, France
Interests: nanopore; single molecule sensing; nanofluidic; biomimetic interfaces; fluorescence; biosensors; nanoscale biophysics; protein at solid/liquid interfaces

Special Issue Information

Dear Colleagues,

The protein adsorption at the solid–liquid interface has a long history, from the origin of life to modern high-performance materials for the industry. It is an old but exciting and active field of research thanks to the various applications to solve societal issues in energy, health or water treatment. Usually, protein adsorption is used as a simple route to improve or give properties to many types of materials, such as catalysts for waste matter degradation or biofuel production, biosensors, improving colloid stability, etc. Protein adsorption is sometimes banned, when it induces membrane fouling or a corona around the nanoparticles. Protein adsorption is also the first step in the response to artificial material in the case of the implants or nanoparticle injections. The broad range of types of protein and the lack of a typical behavior make it an endless topic.

The present Special Issue aims to offer a unique platform to discuss all the aspects of Protein Adsorption on Materials. We intend to cover broad applications involving protein adsorption on material, the protein corona, as well as strategies to reduce fouling by protein. We also aim for contributions on the more fundamental aspects of kinetics, the mechanisms of protein adsorption, as well as the impact on their structure and/or properties. Full articles, short communications, or reviews are welcome.

Assoc. Prof. Sebastien Balme
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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Keywords

  • protein adsorption
  • protein corona
  • hybrid material
  • enzyme immobilisation
  • catalysis
  • biosensor

Published Papers (1 paper)

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Research

11 pages, 2202 KiB  
Article
Revealing the Nanoparticle-Protein Corona with a Solid-State Nanopore
by Diego Coglitore, Pierre Eugene Coulon, Jean-Marc Janot and Sébastien Balme
Materials 2019, 12(21), 3524; https://doi.org/10.3390/ma12213524 - 28 Oct 2019
Cited by 6 | Viewed by 2353
Abstract
Protein adsorption at the liquid–solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein [...] Read more.
Protein adsorption at the liquid–solid interface is an old but not totally solved topic. One challenge is to find an easy way to characterize the protein behavior on nanoparticles and make a correlation with its intrinsic properties. This work aims to investigate protein adsorption on gold nanoparticles and the colloidal properties. The protein panel was chosen from different structural categories (mainly-α, mainly-β or mix-αβ). The result shows that the colloidal stability with salt addition does not depend on the structural category. Conversely, using the single nanopore technique, we show that the mainly-α proteins form a smaller corona than the mainly-β proteins. We assign these observations to the lower internal energy of α-helices, making them more prone to form a homogeneous corona layer. Full article
(This article belongs to the Special Issue Protein Adsorption on Materials and Its Applications)
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