Truncated domains of human serum albumin improves the binding efficiency of uremic toxins: A surface plasmon resonance and computational approach

Aparna Nerusu, Papa Rao Vaikuntapu, Dinesh Kumar Chinthapalli, Appa Rao Podile, Rajagopal Subramanyam

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)1216-1225
Number of pages10
JournalInternational Journal of Biological Macromolecules
Volume155
DOIs
Publication statusPublished - Jul 15 2020

Keywords

  • Domains of human serum albumin
  • Molecular docking
  • Protein bound uremic toxins
  • Protein purifications
  • Protein stability
  • Surface plasmon resonance

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Economics and Econometrics
  • Energy(all)

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