Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin

Journal of Photochemistry and Photobiology. B, Biology
Ajay Kumar Shaw, Samir Kumar Pal

Abstract

Human serum albumin (HSA) is a very important multi-domain transporter protein in the circulatory system responsible for carriage of various kinds of ligands within the physiological system. HSA is also known to undergo conformational transformation at different pH(s) and temperatures. In this report we have studied the binding interactions of a photosensitizing drug, protoporphyrin IX (PPIX) with various conformers of HSA at different temperatures using picosecond time-resolved fluorescence spectroscopy. Also, using dynamic light scattering (DLS) and circular dichroism (CD) spectroscopy we have followed the structural transition of various conformers of HSA at different temperatures. Ensuring the intact binding of PPIX to various conformers of HSA at different temperatures as revealed through time-resolved fluorescence anisotropy decay and significant spectral overlap of emission of Trp214 residue (donor) in domain-IIA and absorption of PPIX (acceptor) bound to domain-IB of HSA, we have applied Förster's resonance energy transfer (FRET) technique to determine the interdomain separation under various environmental conditions. The alkali-induced conformer of HSA shows almost no change in donor-acceptor distance in contrast to th...Continue Reading

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Citations

Jul 9, 2014·European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences·Sajid AsgharQineng Ping
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