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Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin
Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6222512/ https://www.ncbi.nlm.nih.gov/pubmed/30065238 http://dx.doi.org/10.3390/molecules23081915 |
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author | Lemli, Beáta Derdák, Diána Laczay, Péter Kovács, Dorottya Kunsági-Máté, Sándor |
author_facet | Lemli, Beáta Derdák, Diána Laczay, Péter Kovács, Dorottya Kunsági-Máté, Sándor |
author_sort | Lemli, Beáta |
collection | PubMed |
description | Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface. |
format | Online Article Text |
id | pubmed-6222512 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62225122018-11-13 Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin Lemli, Beáta Derdák, Diána Laczay, Péter Kovács, Dorottya Kunsági-Máté, Sándor Molecules Article Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface. MDPI 2018-07-31 /pmc/articles/PMC6222512/ /pubmed/30065238 http://dx.doi.org/10.3390/molecules23081915 Text en © 2018 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lemli, Beáta Derdák, Diána Laczay, Péter Kovács, Dorottya Kunsági-Máté, Sándor Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title | Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title_full | Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title_fullStr | Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title_full_unstemmed | Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title_short | Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin |
title_sort | noncovalent interaction of tilmicosin with bovine serum albumin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6222512/ https://www.ncbi.nlm.nih.gov/pubmed/30065238 http://dx.doi.org/10.3390/molecules23081915 |
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