Binding interaction of a biological photosensitizer with serum albumins: a biophysical study

Chakrabarty, Alok ; Mallick, Arabinda ; Haldar, Basudeb ; Das, Paramita ; Chattopadhyay, Nitin (2007) Binding interaction of a biological photosensitizer with serum albumins: a biophysical study Biomacromolecules, 8 (3). pp. 920-927. ISSN 1525-7797

Full text not available from this repository.

Official URL: http://pubs.acs.org/doi/abs/10.1021/bm061084s

Related URL: http://dx.doi.org/10.1021/bm061084s

Abstract

A photophysical study on the binding interaction of an efficient cancer cell photosensitizer, norharmane (NHM), with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA), has been performed using a combination of steady-state and time-resolved fluorescence techniques. The emission profile undergoes a remarkable change upon addition of the proteins to the buffered aqueous solution of the photosensitizer. The polarity-dependent prototropic transformation is responsible for the remarkable sensitivity of this biological fluorophore to the protein environments. A marked increase in the fluorescence anisotropy in the proteinous environments indicates that the albumin proteins introduce motional restriction on the drug molecule. Light has been thrown on the denaturing action of urea on the probe-bound protein. The probable binding site of the drug in proteins has also been assessed from the combination of denaturation study, micropolarity measurement, and fluorescence resonance energy transfer (FRET) study. The present study suggests that the stability of serum albumins is enhanced upon binding with the drug.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:67406
Deposited On:31 Oct 2011 05:01
Last Modified:31 Oct 2011 05:01

Repository Staff Only: item control page