Spectroscopic Characterization of the Interaction between Dopamine and Human Serum Albumin

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Date
2019-02-27Author
Khalid, Imtiaz M.
Abu Sharkh, Sawsan E.
Samamarh, Husain
Alfaqeeh, Rania
Abuteir, Musa M.
Darwish, Saqer M.
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Show full item recordAbstract
The interactions of HSA with DA have received great attention nowadays due
to its significant effect in the biomedical field and overall health. The main
aim of this work is to examine the interaction between DA and HSA at physiological
conditions. Upon addition of DA to HSA, the fluorescence emission
was quenched with quenching constant Kq = 1.32 × 109 L∙mol−1∙s−1 and the
binding constant of DA with HSA is found to be K = 4.4 × 102 mainly indicating
dynamic quenching. The HSA conformation was altered upon binding
of DA to HSA with an increase in α-helix and a decrease in β-sheets suggesting
unfolding of HSA secondary structure due to weak intermolecular interaction
with HSA. In view of the evidence presented, it is important to understand
the details of the interactions of HSA with DA which will be crucial
in the design of new DA-inspired drugs and help revealing vital details to
better understand the HSA’s role as a transporter for many drugs.