Human serum albumin (HSA), the most abundant protein in plasma, is a monomeric multi-domain macromolecule with nine observed binding sites for endogenous and exogenous ligands. HSA displays an extraordinary ligand binding capacity as a depot and carrier for many compounds including most acidic drugs. Consequently, HSA has the potential to influence the pharmacokinetics and pharmacodynamics of drugs.
Leboffe, L., di Masi, A., Polticelli, F., Trezza, V., Ascenzi, P. (2019). Structural basis of drug recognition by human serum albumin. CURRENT MEDICINAL CHEMISTRY, 26 [10.2174/0929867326666190320105316].
Structural basis of drug recognition by human serum albumin
Leboffe, Loris;di Masi, Alessandra;Polticelli, Fabio;Trezza, Viviana;Ascenzi, Paolo
2019-01-01
Abstract
Human serum albumin (HSA), the most abundant protein in plasma, is a monomeric multi-domain macromolecule with nine observed binding sites for endogenous and exogenous ligands. HSA displays an extraordinary ligand binding capacity as a depot and carrier for many compounds including most acidic drugs. Consequently, HSA has the potential to influence the pharmacokinetics and pharmacodynamics of drugs.File in questo prodotto:
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