Human serum albumin: from bench to bedside.

Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modification, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO-carrier The globular domain structural organization of monomeric HSA is at the root of its allosteric properties which are reminiscent of those of multimeric proteins Here, structural, functional, biotechnological, and biomedical aspects of ligand binding to HSA are summarized

https://iubmb.onlinelibrary.wiley.com/doi/epdf/10.1080/15216540500404093

The extraordinary ligand binding properties of human serum albumin

Interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ), a biologically active molecule, with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA) have been studied using steady state and picosecond time-resolved fluorescence and fluorescence anisotropy. The polarity dependent intramolecular charge transfer (ICT) process is responsible for the remarkable sensitivity of this biological fluorophore to the protein environments. The CT fluorescence exhibits appreciable hypsochromic shift along with an enhancement in the fluorescence yield, fluorescence anisotropy (r) and fluorescence lifetime upon binding with the proteins. The reduction in the rate of ICT within the hydrophobic interior of albumins leads to an increase in the fluorescence yield and lifetime. Marked increase in the fluorescence anisotropy indicates that the probe molecule is located in a motionally constrained environment within the proteins. Micropolarities in the two proteinous environments have been determined following the polarity sensitivity of the CT emission. Addition of urea to the protein-bound systems leads to a reduction in the fluorescence anisotropy indicating the denaturation of the proteins. Polarity measurements and fluorescence resonance energy transfer (FRET) studies throw light in assessing the location of the fluorophore within the two proteinous media.

Spectroscopic investigation on the interaction of ICT probe 3-acetyl-4-oxo-6,7-dihydro-12H Indolo-[2,3-a] quinolizine with serum albumins.

Study of the interaction between icariin and human serum albumin by fluorescence spectroscopy

Fluorescence spectral resolution of tryptophan residues in bovine and human serum albumins.

Competitive binding of phenylbutazone and colchicine to serum albumin in multidrug therapy: A spectroscopic study

Interaction of anticancer drugs with human and bovine serum albumin

Effect of temperature on the methotrexate BSA interaction: Spectroscopic study

The mechanism of cooperative binding of both cytarabine and fluorouracil, used in combination therapy, to the transporting protein [bovine serum albumin (BSA)] has been investigated. Present study shows a strategy of estimating the kind of competition between these drugs with the use of uv and NMR spectroscopy. Two mechanisms of the competition to the transporting protein are proposed. For the quantitative investigations the effect of the protein on both the line width and chemical shifts of the NMR signals of the 5-fluorouracil and cytarabine was analyzed. The pi-pi interaction between the pyrimidine ring of the drugs and the aromatic residues of the protein has been postulated. The binding site for both 5-fluorouracil and cytarabine on BSA was found to be situated in the hydrophobic IIA subdomain. The competition of these two drugs and the removal of 5-fluorouracil by cytarabine from the common binding site in serum albumin tertiary structure are observed.

J. Równicka

Papers

Competitive binding of phenylbutazone and colchicine to serum albumin in multidrug therapy: A spectroscopic study

Interaction of anticancer drugs with human and bovine serum albumin

Effect of temperature on the methotrexate BSA interaction: Spectroscopic study

Competition of drugs to serum albumin in combination therapy.

Effect of urea on serum albumin complex with antithyroid drugs: fluorescence study