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Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface
Albumin is one of the major components of synovial fluid. Due to its negative surface charge, it plays an essential role in many physiological processes, including the ability to form molecular complexes. In addition, glycosaminoglycans such as hyaluronic acid and chondroitin sulfate are crucial com...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9222412/ https://www.ncbi.nlm.nih.gov/pubmed/35741532 http://dx.doi.org/10.3390/e24060811 |
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author | Sionkowski, Piotr Bełdowski, Piotr Kruszewska, Natalia Weber, Piotr Marciniak, Beata Domino, Krzysztof |
author_facet | Sionkowski, Piotr Bełdowski, Piotr Kruszewska, Natalia Weber, Piotr Marciniak, Beata Domino, Krzysztof |
author_sort | Sionkowski, Piotr |
collection | PubMed |
description | Albumin is one of the major components of synovial fluid. Due to its negative surface charge, it plays an essential role in many physiological processes, including the ability to form molecular complexes. In addition, glycosaminoglycans such as hyaluronic acid and chondroitin sulfate are crucial components of synovial fluid involved in the boundary lubrication regime. This study presents the influence of Na [Formula: see text] , Mg [Formula: see text] and Ca [Formula: see text] ions on human serum albumin–hyaluronan/chondroitin-6-sulfate interactions examined using molecular docking followed by molecular dynamics simulations. We analyze chosen glycosaminoglycans binding by employing a conformational entropy approach. In addition, several protein–polymer complexes have been studied to check how the binding site and presence of ions influence affinity. The presence of divalent cations contributes to the decrease of conformational entropy near carboxyl and sulfate groups. This observation can indicate the higher affinity between glycosaminoglycans and albumin. Moreover, domains IIIA and IIIB of albumin have the highest affinity as those are two domains that show a positive net charge that allows for binding with negatively charged glycosaminoglycans. Finally, in discussion, we suggest some research path to find particular features that would carry information about the dynamics of the particular type of polymers or ions. |
format | Online Article Text |
id | pubmed-9222412 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-92224122022-06-24 Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface Sionkowski, Piotr Bełdowski, Piotr Kruszewska, Natalia Weber, Piotr Marciniak, Beata Domino, Krzysztof Entropy (Basel) Article Albumin is one of the major components of synovial fluid. Due to its negative surface charge, it plays an essential role in many physiological processes, including the ability to form molecular complexes. In addition, glycosaminoglycans such as hyaluronic acid and chondroitin sulfate are crucial components of synovial fluid involved in the boundary lubrication regime. This study presents the influence of Na [Formula: see text] , Mg [Formula: see text] and Ca [Formula: see text] ions on human serum albumin–hyaluronan/chondroitin-6-sulfate interactions examined using molecular docking followed by molecular dynamics simulations. We analyze chosen glycosaminoglycans binding by employing a conformational entropy approach. In addition, several protein–polymer complexes have been studied to check how the binding site and presence of ions influence affinity. The presence of divalent cations contributes to the decrease of conformational entropy near carboxyl and sulfate groups. This observation can indicate the higher affinity between glycosaminoglycans and albumin. Moreover, domains IIIA and IIIB of albumin have the highest affinity as those are two domains that show a positive net charge that allows for binding with negatively charged glycosaminoglycans. Finally, in discussion, we suggest some research path to find particular features that would carry information about the dynamics of the particular type of polymers or ions. MDPI 2022-06-10 /pmc/articles/PMC9222412/ /pubmed/35741532 http://dx.doi.org/10.3390/e24060811 Text en © 2022 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 Sionkowski, Piotr Bełdowski, Piotr Kruszewska, Natalia Weber, Piotr Marciniak, Beata Domino, Krzysztof Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title | Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title_full | Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title_fullStr | Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title_full_unstemmed | Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title_short | Effect of Ion and Binding Site on the Conformation of Chosen Glycosaminoglycans at the Albumin Surface |
title_sort | effect of ion and binding site on the conformation of chosen glycosaminoglycans at the albumin surface |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9222412/ https://www.ncbi.nlm.nih.gov/pubmed/35741532 http://dx.doi.org/10.3390/e24060811 |
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