Levosemotiadil, an S-isomer of semotiadil, exhibits stronger binding affinity to human serum albumin (HSA) compared to its R-isomer counterpart. This study utilized high-performance frontal analysis (HPFA) to demonstrate that levosemotiadil binds approximately three times more strongly to HSA than semotiadil. The binding parameters were evaluated using Scatchard analysis, revealing specific interactions with the diazepam binding site on HSA. The presence of diazepam decreased the binding affinity of both enantiomers, while warfarin did not alter their binding characteristics. These findings highlight levosemotiadil's potential as a Ca- and Na-channel blocker with significant binding preferences for HSA, crucial for understanding its pharmacokinetics and therapeutic effects[1].
