Deciphering the perturbation of serum albumins by a ketocyanine dye: a spectroscopic approach

Sarkar, Deboleena ; Mahata, Atanu ; Das, Paramita ; Girigoswami, Agnishwar ; Ghosh, Debanjana ; Chattopadhyay, Nitin (2009) Deciphering the perturbation of serum albumins by a ketocyanine dye: a spectroscopic approach Journal of Photochemistry and Photobiology B: Biology, 96 (2). pp. 136-143. ISSN 1011-1344

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.jphotobiol.2009.05.002

Abstract

Steady state and time resolved fluorometric and circular dichroism (CD) techniques have been exploited to explore the binding interaction of a ketocyanine dye, namely, 2-[3-(N-methyl-N-phenylamino)-2-propenylidene] indanone (MPAPI) with transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). The emission spectrum of buffered solution of the dye is found to be perturbed remarkably upon binding with the proteins. An explicit study with respect to modification of fluorescence and fluorescence anisotropy upon binding, effect of denaturant, fluorescence lifetime and CD measurements reveal that the dye binds with both BSA and HSA; the binding being stronger with the latter. Denaturation and CD studies reveal that stability of the proteins increases upon binding with the dye. The probable binding sites of the dye in the proteinous environments have been assessed from fluorescence resonance energy transfer (FRET) study. The probe is argued to be located in the inter domain cleft region of HSA (near Trp-214). From the similarity in the fluorescence behavior of the dye in BSA and HSA it is inferred that in BSA environment the probe is located near Trp-212 rather than Trp-132.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Serum Albumin; FRET; Circular Dichroism; Fluorescence; Denaturation
ID Code:67484
Deposited On:31 Oct 2011 05:15
Last Modified:31 Oct 2011 05:15

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