Cargando…
Simulations of Protein Adsorption on Nanostructured Surfaces
Recent technological advances have allowed the development of a new generation of nanostructured materials, such as those displaying both mechano-bactericidal activity and substrata that favor the growth of mammalian cells. Nanomaterials that come into contact with biological media such as blood fir...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6423022/ https://www.ncbi.nlm.nih.gov/pubmed/30886353 http://dx.doi.org/10.1038/s41598-019-40920-z |
_version_ | 1783404463983165440 |
---|---|
author | Manzi, Berardo M. Werner, Marco Ivanova, Elena P. Crawford, Russell J. Baulin, Vladimir A. |
author_facet | Manzi, Berardo M. Werner, Marco Ivanova, Elena P. Crawford, Russell J. Baulin, Vladimir A. |
author_sort | Manzi, Berardo M. |
collection | PubMed |
description | Recent technological advances have allowed the development of a new generation of nanostructured materials, such as those displaying both mechano-bactericidal activity and substrata that favor the growth of mammalian cells. Nanomaterials that come into contact with biological media such as blood first interact with proteins, hence understanding the process of adsorption of proteins onto these surfaces is highly important. The Random Sequential Adsorption (RSA) model for protein adsorption on flat surfaces was modified to account for nanostructured surfaces. Phenomena related to the nanofeature geometry have been revealed during the modelling process; e.g., convex geometries can lead to lower steric hindrance between particles, and hence higher degrees of surface coverage per unit area. These properties become more pronounced when a decrease in the size mismatch between the proteins and the surface nanostructures occurs. This model has been used to analyse the adsorption of human serum albumin (HSA) on a nano-structured black silicon (bSi) surface. This allowed the Blocking Function (the rate of adsorption) to be evaluated. The probability of the protein to adsorb as a function of the occupancy was also calculated. |
format | Online Article Text |
id | pubmed-6423022 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-64230222019-03-26 Simulations of Protein Adsorption on Nanostructured Surfaces Manzi, Berardo M. Werner, Marco Ivanova, Elena P. Crawford, Russell J. Baulin, Vladimir A. Sci Rep Article Recent technological advances have allowed the development of a new generation of nanostructured materials, such as those displaying both mechano-bactericidal activity and substrata that favor the growth of mammalian cells. Nanomaterials that come into contact with biological media such as blood first interact with proteins, hence understanding the process of adsorption of proteins onto these surfaces is highly important. The Random Sequential Adsorption (RSA) model for protein adsorption on flat surfaces was modified to account for nanostructured surfaces. Phenomena related to the nanofeature geometry have been revealed during the modelling process; e.g., convex geometries can lead to lower steric hindrance between particles, and hence higher degrees of surface coverage per unit area. These properties become more pronounced when a decrease in the size mismatch between the proteins and the surface nanostructures occurs. This model has been used to analyse the adsorption of human serum albumin (HSA) on a nano-structured black silicon (bSi) surface. This allowed the Blocking Function (the rate of adsorption) to be evaluated. The probability of the protein to adsorb as a function of the occupancy was also calculated. Nature Publishing Group UK 2019-03-18 /pmc/articles/PMC6423022/ /pubmed/30886353 http://dx.doi.org/10.1038/s41598-019-40920-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Manzi, Berardo M. Werner, Marco Ivanova, Elena P. Crawford, Russell J. Baulin, Vladimir A. Simulations of Protein Adsorption on Nanostructured Surfaces |
title | Simulations of Protein Adsorption on Nanostructured Surfaces |
title_full | Simulations of Protein Adsorption on Nanostructured Surfaces |
title_fullStr | Simulations of Protein Adsorption on Nanostructured Surfaces |
title_full_unstemmed | Simulations of Protein Adsorption on Nanostructured Surfaces |
title_short | Simulations of Protein Adsorption on Nanostructured Surfaces |
title_sort | simulations of protein adsorption on nanostructured surfaces |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6423022/ https://www.ncbi.nlm.nih.gov/pubmed/30886353 http://dx.doi.org/10.1038/s41598-019-40920-z |
work_keys_str_mv | AT manziberardom simulationsofproteinadsorptiononnanostructuredsurfaces AT wernermarco simulationsofproteinadsorptiononnanostructuredsurfaces AT ivanovaelenap simulationsofproteinadsorptiononnanostructuredsurfaces AT crawfordrussellj simulationsofproteinadsorptiononnanostructuredsurfaces AT baulinvladimira simulationsofproteinadsorptiononnanostructuredsurfaces |