Albumin–Hyaluronan Interactions: Influence of Ionic Composition Probed by Molecular Dynamics

International Journal of Molecular Sciences

Alina Sionkowska¹  Maciej Przybyłek²  Piotr Bełdowski³  Zbigniew Dendzik⁴  Przemysław Raczyński⁴  Krzysztof Górny⁴  Florian Wieland⁵  Per M. Claesson⁶  Andra Dedinaite⁷ 

[1] Department of Biomaterials and Cosmetics Chemistry, Faculty of Chemistry, Nicolaus Copernicus University in Toruń, Gagarin 7, 87-100 Torun, Poland;Department of Physical Chemistry, Pharmacy Faculty, Collegium Medicum of Bydgoszcz, Nicolaus Copernicus University in Toruń, Kurpińskiego 5, 85-950 Bydgoszcz, Poland;Faculty of Chemical Technology and Engineering, Institute of Mathematics & Physics, Bydgoszcz University of Science & Technology, 85-796 Bydgoszcz, Poland;Faculty of Science and Technology, University of Silesia in Katowice, 75 Pułku Piechoty 1A, 41-500 Chorzow, Poland;Helmholtz-Zentrum Hereon: Institute for metallic Biomaterials, Max-Planck-Straße 1, 21502 Geesthacht, Germany;KTH Royal Institute of Technology, Department of Chemistry, Surface and Corrosion Science, School of Engineering Sciences in Chemistry, Biotechnology and Health, SE-100 44 Stockholm, Sweden;KTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Engineering Pedagogics, SE-100 44 Stockholm, Sweden;

关键词: hyaluronic acid;    hyaluronan;    human serum albumin;    molecular dynamics simulations;    hydrogen bonds;    water mediated interactions;   

DOI  :  10.3390/ijms222212360

来源: DOAJ

【 摘 要 】

The lubrication mechanism in synovial fluid and joints is not yet fully understood. Nevertheless, intermolecular interactions between various neutral and ionic species including large macromolecular systems and simple inorganic ions are the key to understanding the excellent lubrication performance. An important tool for characterizing the intermolecular forces and their structural consequences is molecular dynamics. Albumin is one of the major components in synovial fluid. Its electrostatic properties, including the ability to form molecular complexes, are closely related to pH, solvation, and the presence of ions. In the context of synovial fluid, it is relevant to describe the possible interactions between albumin and hyaluronate, taking into account solution composition effects. In this study, the influence of Na⁺, Mg²⁺, and Ca²⁺ ions on human serum albumin–hyaluronan interactions were examined using molecular dynamics tools. It was established that the presence of divalent cations, and especially Ca²⁺, contributes mostly to the increase of the affinity between hyaluronan and albumin, which is associated with charge compensation in negatively charged hyaluronan and albumin. Furthermore, the most probable binding sites were structurally and energetically characterized. The indicated moieties exhibit a locally positive charge which enables hyaluronate binding (direct and water mediated).

【 授权许可】

Unknown