Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Sionkowski, Piotr, Bełdowski, Piotr, Kruszewska, Natalia, Weber, Piotr, Marciniak, Beata, Domino, Krzysztof
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
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
_version_ 1784732867678437376
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
work_keys_str_mv AT sionkowskipiotr effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface
AT bełdowskipiotr effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface
AT kruszewskanatalia effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface
AT weberpiotr effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface
AT marciniakbeata effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface
AT dominokrzysztof effectofionandbindingsiteontheconformationofchosenglycosaminoglycansatthealbuminsurface