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dc.contributor.authorMorales-Toyo, Miguel
dc.contributor.authorGlidewell, Christopher
dc.contributor.authorBruno-Colmenares, Julia
dc.contributor.authorCubillán, Néstor
dc.contributor.authorSánchez-Colls, Ronald
dc.contributor.authorAlvarado, Ysaias
dc.contributor.authorRestrepo, Jelen
dc.identifier.citationMorales-Toyo , M , Glidewell , C , Bruno-Colmenares , J , Cubillán , N , Sánchez-Colls , R , Alvarado , Y & Restrepo , J 2019 , ' Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods ' , Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy , vol. In press .
dc.identifier.otherRIS: urn:E8AB034052EFD9D53B1A12402077E0B9
dc.descriptionThe authors thank Fondo Nacional de Ciencia Tecnología e Innovación (FONACIT Proyecto de apoyo a Grupos No. G-2005000403). Proyecto 1063, Instituto Venezolano de Investigaciones Científicas (IVIC).en
dc.description.abstractA novel hydrazone, (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate (EFHB), has been synthesized and characterized by FT-IR, NMR and Mass spectroscopy, and X-ray diffraction; compound crystallized as translucent light yellow thin plates. EFHB was studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Addition of this hydrazone to HSA produced significant fluorescence quenching and splitting of emission spectra of HSA through static quenching mechanism with binding constants of about 104 M−1 at 292.15, 298.15, 304.15 and 310.15 K. According to the synchronous fluorescence, tryptophan and tyrosine residues of the protein are most perturbed by the binding process. Thermodynamic parameters ΔG, ΔH, and ΔS were got and the main sort of acting force between EFHB and HSA was studied. Results of molecular docking have shown that EFHB binds to subdomain IIA of HSA mainly by hydrophobic interaction, energy binding are in good agreement with those obtained by fluorescence study (ΔGthe = −7.32 ± 0.09 kcal mol−1 and ΔGexp = −6.76 ± 0.03 kcal mol−1).
dc.relation.ispartofSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopyen
dc.subjectHydrazone derivativeen
dc.subjectCrystal structureen
dc.subjectMolecular dockingen
dc.subjectFluorescence spectroscopyen
dc.subjectQD Chemistryen
dc.titleSynthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methodsen
dc.typeJournal articleen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.description.statusPeer revieweden

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