Interactions of Different Urolithins With Bovine Serum Albumin

Backgound/Objectives Urolithins (UROs) are the metabolites derived from gut microbial action on ellagitannins and ellagic acid-rich foods. Following their absorption in intestine, UROs transported through systemic circulation to various tissues where they can express biological function as antimicrobial, anti-inflammatory, anticancer agents. In addition blood plasma, be found glucuronide sulfate conjugates, also urine. Therefore, interactions of with serum proteins great clinical interest. Methods A powerful technique for examining these urolithin-serum protein is fluorescence spectroscopy. Bovine albumin (BSA) a particularly suitable model because it readily available, affordable, similar human albumin. This work aimed study binding (urolithin A, UROA urolithin B, UROB) conjugates (UROAG UROBG) BSA by quenching intrinsic protein. Results The spectra obtained showed that process influenced polyphenol's structure conjugation glucuronide. calculated Stern Vollmer constants (K sv ): UROB K were 59236 ± 5706 69653 14922, respectively, while UROAG UROBG, values 15179 2770 9462 1955, which affinity decreased glucuronidation. Molecular docking studies confirmed all studied molecules will bind favorably BSA. preferential site both UROGs Sudlow I, II. URO-Gs cleft region lower scores than I site. Conclusion aglycone's higher hydrophobicity increases BSA, thus reducing its bioavailability blood.