Submitted in fulfilment of the requirements of the Degree of Master of Technology: Chemistry, Durban University of Technology, 2012. / The present work involves the interaction studies of chiral compounds with the
Human Serum Albumin (HSA) protein using computational and experimental
methods. The HSA protein has multiple binding sites that forms the basis for its
exceptional ability to interact with many organic and inorganic molecules, which
makes this protein an important regulator of intercellular fluxes and the
pharmacokinetic behaviour of many drugs. This study was undertaken to evaluate the
related pharmacokinetic and enantioselective binding parameters of the racemic
catechin enantiomers with the HSA. Accordingly, this work involved a method
development for the chiral separation of a racemic compound, by capillary
electrophoresis-electrokinetic chromatography (CE-EKC) with a highly sulphated
beta-cyclodextrin (HS--CD) as a chiral selector. The experimental work was
supported by two molecular docking studies. The first included the mimicking of the
host-guest interactions between a chiral selector and an enantiomeric compound. The
second study included the estimation of the pseudo enantioselective (ES) binding of
catechin to HSA.
Overall, it was found that CE-EKC is the preferred method for the(±)-catechin
binding to HSA protein evaluation. Moreover, the technique used in this work is not
restricted to HSA or polyphenols, but can also be applied to other proteins and
ligands that possess chirality. Furthermore, the molecular docking approaches also
proved to be very useful for the evaluation of chiral recognition systems and for
elucidation of the ligand-protein interactions.
| Identifer | oai:union.ndltd.org:netd.ac.za/oai:union.ndltd.org:dut/oai:localhost:10321/879 |
| Date | 30 July 2013 |
| Creators | Sabela, Myalowenkosi Innocent |
| Contributors | Bisetty, Krishna |
| Source Sets | South African National ETD Portal |
| Language | English |
| Detected Language | English |
| Type | Thesis |
| Format | 185 p |
Page generated in 0.0018 seconds