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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...

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Autores principales: Lemli, Beáta, Derdák, Diána, Laczay, Péter, Kovács, Dorottya, Kunsági-Máté, Sándor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
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.
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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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