Journal
JOURNAL OF CHEMICAL SCIENCES
Volume 119, Issue 2, Pages 77-82Publisher
INDIAN ACAD SCIENCES
DOI: 10.1007/s12039-007-0013-9
Keywords
fluorescence resonance energy transfer; photosensitisation; human serum albumin; fluorescence quenching; overlap integral; Stern-Volmer constant
Categories
Ask authors/readers for more resources
The interaction between a bioactive molecule, 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ), with human serum albumin (HSA) has been studied using steady-state absorption and fluorescence techniques. A I : I complex formation has been established and the binding constant (K) and free energy change for the process have been reported. The AODIQ-HSA complex results in fluorescence resonance energy transfer (FRET) from the tryptophan moiety of HSA to the probe. The critical energy-transfer distance (R-0) for FRET and the Stern-Volmer constant (K-sv) for the fluorescence quenching of the donor in the presence of the acceptor have been determined. Importantly, K-sv has been shown to be equal to the binding constant itself, implying that the fluorescence quenching arises only from the FRET process. The study suggests that the donor and the acceptor are bound to the same protein at different locations but within the quenching distance.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available