Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)

Nitin Kumar Pandey, Sudeshna Ghosh, Nóra Veronika Nagy, Swagata Dasgupta

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Protein aggregation is related to a series of pathological disorders the main cause of which are the fibrillar species generated during the process. Human serum albumin (HSA) undergoes rapid fibrillation in the presence of Cu(II) at pH 7.4 in 60% ethanol after 6-h incubation (~65 °C) followed by room temperature incubation. Here, we have investigated the effect of a stoichiometric variation of Cu(II) on the self-assembly of HSA using Congo red and thioflavin T dye-binding studies, circular dichroism spectroscopy, Fourier transform infrared spectroscopy, electron paramagnetic resonance spectroscopy, fluorescence microscopy and transmission electron microscopy. The simulation of EPR spectra suggests that with the increment in Cu(II) ion concentration, there is a change in ligand field coordination. Kinetic parameters indicate reduced cooperativity that may be related to the nonspecific coordination on increment of Cu(II) concentration. Cu(II) is also able to direct the accumulation of a large number of fibers along with a formation of dense fibrillar network which is evident from microscopic images.

Original languageEnglish
Pages (from-to)1366-1378
Number of pages13
JournalJournal of Biomolecular Structure and Dynamics
Volume32
Issue number9
DOIs
Publication statusPublished - Sep 2 2014

Keywords

  • Aggregation
  • Cu(II)
  • Fibrillation
  • Human serum albumin
  • Stoichiometry

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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