Spectroscopic and thermodynamic characterization of the interaction of a new synthesized antitumor drug candidate 2H4MBBH with human serum albumin

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creativework.keywords2H4MBBH, drug binding, fluorescence spectroscopy, human serum albumin, quenching
creativework.publisherPensoft Publishersen
dc.contributor.authorAbarova S.
dc.contributor.authorStoitchkova K.
dc.contributor.authorTzonev S.
dc.contributor.authorArgirova M.
dc.contributor.authorYancheva D.
dc.contributor.authorAnastassova N.
dc.contributor.authorTenchov B.
dc.date.accessioned2024-07-10T14:27:06Z
dc.date.accessioned2024-07-10T14:51:07Z
dc.date.available2024-07-10T14:27:06Z
dc.date.available2024-07-10T14:51:07Z
dc.date.issued2024-01-01
dc.description.abstractIn 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.
dc.identifier.doi10.3897/pharmacia.71.e112385
dc.identifier.issn0428-0296
dc.identifier.scopusSCOPUS_ID:85185320188en
dc.identifier.urihttps://rlib.uctm.edu/handle/123456789/903
dc.language.isoen
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85185320188&origin=inward
dc.titleSpectroscopic and thermodynamic characterization of the interaction of a new synthesized antitumor drug candidate 2H4MBBH with human serum albumin
dc.typeArticle
oaire.citation.volume71
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