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Characterisation by fluorescence of human and bovine serum albumins in interaction with eosin Y

C. CHILOM1, G. BARANGĂ1, D. GĂZDARU1, A. POPESCU1,*

Affiliation

  1. Research Centre in Molecular Biophysics, Faculty of Physics, University of Bucharest, Măgurele, Romania

Abstract

Human and bovine serum albumins (HSA and BSA) are blood proteins involved in interactions with various types of molecules (e.g. hormones, fatty acids, drugs). This paper is approaching the albumin interactions with eosin Y, a fluorescent red dye usually used to stain cytoplasm, collagen and muscle fibres. Our experiments were focussed on spectroscopic and thermodynamic characterisation of albumins-eosin Y interactions. The experiments were performed both in Hepes and TrisHCl buffers, at two temperatures (26 °C and 36 °C) and at pH 7.4. It was observed that the Stern-Volmer constants have larger values in Hepes than in Tris-HCl buffer presenting changes with temperature. The strength of the interactions was characterised by the affinity constants (KA). The affinity constants are one order of magnitude greater for eosin Y interactions with HSA in Hepes than those in Tris-HCl buffer. The stoichiometry shows that there are two binding sites on BSA and one on HSA. The thermodynamic parameters (∆G, ∆H, ∆S and ∆Cp) show that both proteins are involved in spontaneous interactions with the dye, these processes being driven by entropy. The caloric capacity variation is greater for the BSA-eosin Y interaction than for the case of HSA-eosin Y interaction..

Keywords

Albumins, Eosin Y, Fluorescence.

Submitted at: Jan. 18, 2013
Accepted at: April 11, 2013

Citation

C. CHILOM, G. BARANGĂ, D. GĂZDARU, A. POPESCU, Characterisation by fluorescence of human and bovine serum albumins in interaction with eosin Y, Journal of Optoelectronics and Advanced Materials Vol. 15, Iss. 3-4, pp. 311-316 (2013)