Silymarin is a flavonolignan complex mixture found in the fruits of milk thistle (<i>Silybum marianum </i>L), a member of the Asteraceae family. It has been in clinical use for many years in Europe, Asia, United States and Africa as a hepatoprotective and potent antioxidant. Due to its poor water solubility, the bioavailability of silymarin is low. Human serum albumin (HSA) is the most abundant carrier protein of the body with a high affinity for a wide range of metabolites and drugs and responsible to bring such solutes into the blood stream and then deliver them to the target organs. It is possible that dietary silymarin can form serum albumin conjugates to modulate its bioavailability. It is thus pertinent to consider the specific binding of these compounds to HSA. Individual isomers of silymarin (silybin A, silybin B, iso-silybin A, iso-silybin B, silychristin, and silydianin) were investigated for their ability to bind to (HSA) using UV-Vis, Fluorescence and circular dichroism (CD) techniques. All experiments showed ligand binding affinity to HSA, but was different among the six examined isomers. These results were compared with molecular modeling docking computations using Sybyl-X 2.1.1 molecular modeling software. Docking studies reveal that the individual molecules lie within hydrogen bonding distance of Trp 214 residue subdomains IB and IIA and IIIA.

Binding of silymarin flavolignan isomers to human serum albumin: Experimental and computational studies

255th National Meeting (2018)

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