Modulation of accessibility of subdomain IB in the pH-dependent interaction of bovine serum albumin with cochineal red A: A combined view from spectroscopy and docking simulations

Priyanka Bolel, Niharendu Mahapatra, Shubhashis Datta, Mintu Halder

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

Our recent report on the binding of Cochineal Red A, a food dye, with HSA and BSA at pH 7.4 has revealed that electrostatic forces is the principal cause of interaction. In that study issues relating to complications arising out of modulation of dye binding affinity of BSA with pH had not been explored. Here we have further explored the interaction of Cochineal Red A with BSA in pH range 4.8-7.8. Surprisingly, this system behaves differently in the texture of interaction pattern at two extremes of studied pH range, unlike HSA. Importantly, the charge on the amino acid side chains in the binding pocket is likely to play a significant role.

Original languageEnglish
Pages (from-to)4606-4613
Number of pages8
JournalJournal of Agricultural and Food Chemistry
Volume61
Issue number19
DOIs
StatePublished - 15 May 2013
Externally publishedYes

Keywords

  • BSA
  • differential accessibility
  • electrostatic interaction
  • food dye
  • molecular docking

ASJC Scopus subject areas

  • Chemistry (all)
  • Agricultural and Biological Sciences (all)

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