+44 (0)1509 263171
Please use this identifier to cite or link to this item:
|Title: ||The use of long wavelength fluorescence in the study of ligand-protein interactions|
|Authors: ||Brown, Marc B.|
|Issue Date: ||1993|
|Publisher: ||© M.B. Brown|
|Abstract: ||The binding of a drug or other ligand to plasma proteins can effect their
absorption, metabolism and excretion which can lead to a change in its toxicity
and therapeutic action. Fluorescence is a technique that has been used to study
such interactions and has the advantages of extreme sensitivity and specificity.
Previously fluorescence has been monitored in the UV /vis range of the spectrum.
However, a new development is long wavelength fluorescence (600-1000nm),
which has the added benefits of a lower background, decreased scattering,
decreased photodecomposition and the availability of inexpensive, solid state,
Certain dyes including polymethines, xanthenes and phenoxazines that fluoresce
in the long wavelength region (600-1000nm) of the spectrum were investigated for
use as fluorescence probes.
Nile Red, a strongly hydrophobic phenoxazine dye, was found to have an emission
wavelength and intensity which was strongly dependent on the polarity of its
environment. Consequently, it was bound to certain proteins including bovine and
human serum albumin, aI-acid glycoprotein and B-lactoglobulin and provided both
qualitative and quantitative information on the nature and type of binding site on
the protein. It was also used in the study of ligand protein binding interactions in
which competition for a binding site on the protein occurs between the probe and
other ligands such as drugs or fatty acids.
The project also involved a preliminary investigation into a novel double probe
technique for the study of drug-protein interactions and the development of a flow
injection analysis method involving gradient titration of a drug against a
|Description: ||A Doctoral Thesis. Submitted in partial fulfilment of the requirements for the award of Doctor of Philosophy of Loughborough University|
|Appears in Collections:||PhD Theses (Chemistry)|
Files associated with this item:
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.