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Fasano, M., Curry, S., Terreno, E., Galliano, M., Fanali, G., Narciso, P., Notari, S. and Ascenzi, P. (2005) The Extraordinary Ligand Binding Properties of Human Serum Albumin. IUBMB Life, 57, 787-796.
https://doi.org/10.1080/15216540500404093

has been cited by the following article:

• TITLE: Spectroscopic Characterization of the Interaction between Dopamine and Human Serum Albumin

  AUTHORS: Imtiaz M. Khalid, Sawsan E. Abu Sharkh, Husain Samamarh, Rania Alfaqeeh, Musa M. Abuteir, Saqer M. Darwish

  KEYWORDS: Dopamine, HSA, Binding Constant, Non-Linear Stern-Volmer Plot, Protein Secondary Structure, FT-IR Spectroscopy

  JOURNAL NAME: Open Journal of Biophysics, Vol.9 No.2, February 27, 2019

  ABSTRACT: 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.