Unveiling the stimulatory effects of tartrazine on human and bovine serum albumin fibrillogenesis: Spectroscopic and microscopic study

Al-Shabib, N.A. and Khan, J.M. and Alsenaidy, M.A. and Alsenaidy, A.M. and Khan, M.S. and Husain, F.M. and Khan, M.R and Naseem, M. and Sen, P. and Alam, P. and Khan, R.H. (2018) Unveiling the stimulatory effects of tartrazine on human and bovine serum albumin fibrillogenesis: Spectroscopic and microscopic study. Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 191. pp. 116-124. ISSN 13861425

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Abstract

Amyloid fibrils are playing key role in the pathogenesis of various neurodegenerative diseases. Generally anionic molecules are known to induce amyloid fibril in several proteins. In this work, we have studied the effect of anionic food additive dye i.e., tartrazine (TZ) on the amyloid fibril formation of human serum albumins (HSA) and bovine serum albumin (BSA) at pHs 7.4 and 3.5. We have employed various biophysical methods like, turbidity measurements, Rayleigh Light Scattering (RLS), Dynamic Light Scattering (DLS), intrinsic fluorescence, Congo red assay, far-UV CD, transmission electron microscopy (TEM) and atomic force microscopy (AFM) to decipher the mechanism of TZ-induce amyloid fibril formation in both the serum albumins at pHs 7.4 and 3.5. The obtained results suggest that both the albumins forms amyloid-like aggregates in the presence of 1.0 to 15.0 mM of TZ at pH 3.5, but no amyloid fibril were seen at pH 7.4. The possible cause of TZ-induced amyloid fibril formation is electrostatic and hydrophobic interaction because sulfate group of TZ may have interacted electrostatically with positively charged amino acids of the albumins at pH 3.5 and increased protein-protein and protein-TZ interactions leading to amyloid fibril formation. The TEM, RLS and DLS results are suggesting that BSA forms bigger size amyloids compared to HSA, may be due to high surface hydrophobicity of BSA.

Item Type: Article
Uncontrolled Keywords: Amyloid fibril; Food additive dye; Human and bovine serum albumin; pH; Protein aggregation; Tartrazine (TZ)
Subjects: R Medicine > R Medicine (General)
Divisions: Centres > Interdisciplinary Biotechnology Unit
Depositing User: AMU Library
Date Deposited: 20 Jan 2018 06:43
Last Modified: 11 Feb 2018 12:59
URI: http://ir.amu.ac.in/id/eprint/10883

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