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Truncated domains of human serum albumin improves the binding efficiency of uremic toxins: A surface plasmon resonance and computational approach.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2020 Jul 15; Vol. 155, pp. 1216-1225. Date of Electronic Publication: 2019 Nov 15. - Publication Year :
- 2020
-
Abstract
- Albumin binding is the major cause for the toxicity of protein bound uremic toxins (PBUTs) in uremic patients. Albumin binding property is exploited to address this issue, as some of the extracorporeal dialysis systems use albumin as dialysate. In this line, a detailed study about binding of PBUTs to human serum albumin (HSA) and its domains gives valuable information. The focus of this work emphasizes the mechanism of binding of HSA and its domains with a few selected PBUTs such as hippuric acid (HA), indole acetic acid (IAA) and melatonin. The HSA domains (D2, D3 and D2-3) were expressed in Pichia pastoris and purified by using Albupure matrix. The binding of the expressed domains and HSA, with PBUTs, was measured using surface plasmon resonance and analyzed. All the three domains have significant affinity towards PBUTs, while D3 had greater affinity for all the three selected PBUTs. Docking studies showed that the basic amino acid, lysine, was forming hydrogen bond with PUBTs inorder to stabile these complex. This study would be having therapeutic importance for preparing the extracorporeal dialysis systems, in combination of different domains of HSA to remove the PBUTs.<br /> (Copyright © 2019 Elsevier B.V. All rights reserved.)
- Subjects :
- Dialysis Solutions
Humans
Molecular Docking Simulation
Protein Binding
Renal Dialysis
Saccharomycetales genetics
Saccharomycetales metabolism
Serum Albumin, Human chemistry
Surface Plasmon Resonance
Toxins, Biological blood
Uremia blood
Hippurates metabolism
Indoleacetic Acids metabolism
Melatonin metabolism
Protein Domains
Serum Albumin, Human metabolism
Toxins, Biological metabolism
Uremia therapy
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 155
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 31734369
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2019.11.089