Structural basis of the drug-binding specificity of human serum albumin.

By J. Ghuman, P. Zunszain, I. Petitpas, A. A. Bhattacharya, M. Otagiri, S. Curry. Journal of Molecular Biology, 2005

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A Review of the Common Neurodegenerative Disorders: Current Therapeutic Approaches and the Potential Role of Nanotherapeutics (2022, background): “Some drugs are highly bound to these proteins, thereby limiting the amount of the drug available in circulation, ultimately reducing the free drug available for transportation to the brain [84].”
Trend Analysis of a Database of Intravenous Pharmacokinetic Parameters in Humans for 670 Drug Compounds (2008, background): “higher binding relative to bases and neutrals due to an ion-pair interaction with a basic residue within albumin (Ghuman et al., 2005).”
The influence of lipophilicity in drug discovery and design (2012, background): “Acidic compounds have higher protein binding relative to bases and neutrals due to an ionpair interaction with a basic residue within serum albumin [77].”
Structures of bovine, equine and leporine serum albumin. (2012, background): “The amino acids in the Sudlow drug-binding sites DSI and DSII concurrently create pockets for FA7 and FA3/FA4, respectively (Ghuman et al., 2005).”