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Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates
Superhydrophilic and superhydrophobic substrates are widely known to inhibit the attachment of a variety of motile and/or nonmotile bacteria. However, the thermodynamics of attachment are complex. Surface energy measurements alone do not address the complexities of colloidal (i.e., bacterial) disper...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538270/ https://www.ncbi.nlm.nih.gov/pubmed/34681201 http://dx.doi.org/10.3390/ph14100977 |
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author | Cavitt, T. Brian Pathak, Niyati |
author_facet | Cavitt, T. Brian Pathak, Niyati |
author_sort | Cavitt, T. Brian |
collection | PubMed |
description | Superhydrophilic and superhydrophobic substrates are widely known to inhibit the attachment of a variety of motile and/or nonmotile bacteria. However, the thermodynamics of attachment are complex. Surface energy measurements alone do not address the complexities of colloidal (i.e., bacterial) dispersions but do affirm that polar (acid-base) interactions ([Formula: see text]) are often more significant than nonpolar (Lifshitz-van der Waals) interactions ([Formula: see text]). Classical DLVO theory alone also fails to address all colloidal interactions present in bacterial dispersions such as [Formula: see text] and Born repulsion ([Formula: see text]) yet accounts for the significant electrostatic double layer repulsion ([Formula: see text]). We purpose to model both motile (e.g., P. aeruginosa and E. coli) and nonmotile (e.g., S. aureus and S. epidermidis) bacterial attachment to both superhydrophilic and superhydrophobic substrates via surface energies and extended DLVO theory corrected for bacterial geometries. We used extended DLVO theory and surface energy analyses to characterize the following Gibbs interaction energies for the bacteria with superhydrophobic and superhydrophilic substrates: [Formula: see text] , [Formula: see text] , [Formula: see text] , and [Formula: see text]. The combination of the aforementioned interactions yields the total Gibbs interaction energy ([Formula: see text]) of each bacterium with each substrate. Analysis of the interaction energies with respect to the distance of approach yielded an equilibrium distance ([Formula: see text]) that seems to be independent of both bacterial species and substrate. Utilizing both [Formula: see text] and Gibbs interaction energies, substrates could be designed to inhibit bacterial attachment. |
format | Online Article Text |
id | pubmed-8538270 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-85382702021-10-24 Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates Cavitt, T. Brian Pathak, Niyati Pharmaceuticals (Basel) Article Superhydrophilic and superhydrophobic substrates are widely known to inhibit the attachment of a variety of motile and/or nonmotile bacteria. However, the thermodynamics of attachment are complex. Surface energy measurements alone do not address the complexities of colloidal (i.e., bacterial) dispersions but do affirm that polar (acid-base) interactions ([Formula: see text]) are often more significant than nonpolar (Lifshitz-van der Waals) interactions ([Formula: see text]). Classical DLVO theory alone also fails to address all colloidal interactions present in bacterial dispersions such as [Formula: see text] and Born repulsion ([Formula: see text]) yet accounts for the significant electrostatic double layer repulsion ([Formula: see text]). We purpose to model both motile (e.g., P. aeruginosa and E. coli) and nonmotile (e.g., S. aureus and S. epidermidis) bacterial attachment to both superhydrophilic and superhydrophobic substrates via surface energies and extended DLVO theory corrected for bacterial geometries. We used extended DLVO theory and surface energy analyses to characterize the following Gibbs interaction energies for the bacteria with superhydrophobic and superhydrophilic substrates: [Formula: see text] , [Formula: see text] , [Formula: see text] , and [Formula: see text]. The combination of the aforementioned interactions yields the total Gibbs interaction energy ([Formula: see text]) of each bacterium with each substrate. Analysis of the interaction energies with respect to the distance of approach yielded an equilibrium distance ([Formula: see text]) that seems to be independent of both bacterial species and substrate. Utilizing both [Formula: see text] and Gibbs interaction energies, substrates could be designed to inhibit bacterial attachment. MDPI 2021-09-26 /pmc/articles/PMC8538270/ /pubmed/34681201 http://dx.doi.org/10.3390/ph14100977 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cavitt, T. Brian Pathak, Niyati Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title | Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title_full | Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title_fullStr | Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title_full_unstemmed | Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title_short | Modeling Bacterial Attachment Mechanisms on Superhydrophobic and Superhydrophilic Substrates |
title_sort | modeling bacterial attachment mechanisms on superhydrophobic and superhydrophilic substrates |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8538270/ https://www.ncbi.nlm.nih.gov/pubmed/34681201 http://dx.doi.org/10.3390/ph14100977 |
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