Abarova S.Stoitchkova K.Tzonev S.Argirova M.Yancheva D.Anastassova N.Tenchov B.2024-07-102024-07-102024-07-102024-07-102024-01-010428-029610.3897/pharmacia.71.e112385SCOPUS_ID:85185320188https://rlib.uctm.edu/handle/123456789/903In the present work we studied the interactions of a newly synthesized drug candidate, 2-(2-hydroxy-4-methoxyben-zylidene)-1-(1H-benzimidazol-2-yl)hydrazine (2H4MBBH), with human serum albumin (HSA) by fluorescence spectroscopy. 2H4MBBH-HSA binding parameters were assessed by fluorescence quenching strategy. As made clear by the concentration data, 2H4MBBH unequivocally quenched the instrinsic HSA fluorescence. The calculated Stern-Volmer quenching constant Ksv, the Ka of 2H4MBBH-HSA complexes, as well as the thermodynamic parameters ΔH°, ΔS° and ΔG°, showed that the H-bonding forces play major part in the interaction of 2H4MBBH with HSA. These calculations point to a quenching component based on 2H4MBBH-HSA static complex formation rather than energetic collisions.enArticle