Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: a spectroscopic study.
In the present work, we have studied the interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde (HN12) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) by steady state absorption and emission spectroscopy combined with time resolved fluorescence measurements. The measured binding constant (K) and free energy change (DeltaG) indicate a stronger affinity of HN12 molecule for HSA than BSA. Steady state anisotropy, excitation anisotropy and fluorescence resonance energy transfer (FRET) studies indicate that the probe molecule resides at the hydrophobic site of the protein environment.
Balia Singh
Rupashree
R
Department of Chemistry, University of Calcutta, 92 A.P.C. Road, Kolkata 700 009, India.
Mahanta
Subrata
S
Guchhait
Nikhil
N
D000818:Animals; D016880:Anisotropy; D002417:Cattle; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D009281:Naphthalenes / Q000378:metabolism*; D011485:Protein Binding; D011522:Protons; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D009281:Naphthalenes; D011522:Protons; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; C062247:2-hydroxy-1-naphthaldehyde