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The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study

BACKGROUND: Human serum albumin (HSA) is a valuable component of non-enzymatic and endogenous antioxidant mechanisms. The antioxidant activity of HSA can be modulated by ligands, including drugs. Although this is a central topic in the field of oxidation, there is still a lack of information about t...

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Autores principales: Rogóż, Wojciech, Mac, Kinga, Owczarzy, Aleksandra, Kulig, Karolina, Pożycka, Jadwiga, Maciążek-Jurczyk, Małgorzata
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer International Publishing 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539444/
https://www.ncbi.nlm.nih.gov/pubmed/37704832
http://dx.doi.org/10.1007/s43440-023-00529-6
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author Rogóż, Wojciech
Mac, Kinga
Owczarzy, Aleksandra
Kulig, Karolina
Pożycka, Jadwiga
Maciążek-Jurczyk, Małgorzata
author_facet Rogóż, Wojciech
Mac, Kinga
Owczarzy, Aleksandra
Kulig, Karolina
Pożycka, Jadwiga
Maciążek-Jurczyk, Małgorzata
author_sort Rogóż, Wojciech
collection PubMed
description BACKGROUND: Human serum albumin (HSA) is a valuable component of non-enzymatic and endogenous antioxidant mechanisms. The antioxidant activity of HSA can be modulated by ligands, including drugs. Although this is a central topic in the field of oxidation, there is still a lack of information about the protection against the effects of elevated free radical levels. METHODS: The aim of this study was to investigate the antioxidant activity of kanamycin (KAN) and neomycin (NEO) and their effect on the antioxidant potential of HSA using spectroscopic and microcalorimetric techniques. RESULTS: Despite the fact that kanamycin and neomycin interact with HSA, no changes in the secondary structure of the protein have been observed. The analysis of the aminoglycoside antibiotics showed their low antioxidant activity and a synergistic effect of the interaction, probably due to the influence of ligands (KAN, NEO) on the availability of HSA amino acid residues functional groups, such as the free thiol group (Cys-34). CONCLUSIONS: Based on the spectroscopic and microcalorimetric data, both KAN and NEO can be considered modulators of the HSA antioxidant activity.
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spelling pubmed-105394442023-09-30 The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study Rogóż, Wojciech Mac, Kinga Owczarzy, Aleksandra Kulig, Karolina Pożycka, Jadwiga Maciążek-Jurczyk, Małgorzata Pharmacol Rep Article BACKGROUND: Human serum albumin (HSA) is a valuable component of non-enzymatic and endogenous antioxidant mechanisms. The antioxidant activity of HSA can be modulated by ligands, including drugs. Although this is a central topic in the field of oxidation, there is still a lack of information about the protection against the effects of elevated free radical levels. METHODS: The aim of this study was to investigate the antioxidant activity of kanamycin (KAN) and neomycin (NEO) and their effect on the antioxidant potential of HSA using spectroscopic and microcalorimetric techniques. RESULTS: Despite the fact that kanamycin and neomycin interact with HSA, no changes in the secondary structure of the protein have been observed. The analysis of the aminoglycoside antibiotics showed their low antioxidant activity and a synergistic effect of the interaction, probably due to the influence of ligands (KAN, NEO) on the availability of HSA amino acid residues functional groups, such as the free thiol group (Cys-34). CONCLUSIONS: Based on the spectroscopic and microcalorimetric data, both KAN and NEO can be considered modulators of the HSA antioxidant activity. Springer International Publishing 2023-09-13 2023 /pmc/articles/PMC10539444/ /pubmed/37704832 http://dx.doi.org/10.1007/s43440-023-00529-6 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Rogóż, Wojciech
Mac, Kinga
Owczarzy, Aleksandra
Kulig, Karolina
Pożycka, Jadwiga
Maciążek-Jurczyk, Małgorzata
The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title_full The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title_fullStr The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title_full_unstemmed The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title_short The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
title_sort effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539444/
https://www.ncbi.nlm.nih.gov/pubmed/37704832
http://dx.doi.org/10.1007/s43440-023-00529-6
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