title: 3,6-diHydroxyflavone/bovine serum albumin interaction in cyclodextrin medium: absorption and emission monitoring.
abstract: Photophysical properties of a bioactive flavonol which can be used as a model for polyhydroxylated natural flavonols, 3,6-diHydroxyflavone (3,6-diHF) in cyclodextrins (CDs)/bovine serum albumin (BSA) systems have been studied by absorption and fluorescence spectroscopy. The influence of CDs nature and of the different molar ratios BSA/CDs on the fluorescent characteristics of 3,6-diHF, and on the excited - state intramolecular proton transfer (ESIPT) process were studied. Quantitative information on the interaction between 3,6-diHF and BSA in CDs medium, were estimated. The influence of temperature (25-60°C range) on the intrinsic fluorescence of BSA in 3,6-diHF/BSA/CDs systems, was investigated. The results are discussed with relevance to 3,6-diHF as a potential sensitive fluorescence probe in the systems of biological interest.
authors.affiliation: Romanian Academy, Institute of Physical Chemistry "Ilie Murgulescu", Splaiul Independentei 202, 060021 Bucharest, Romania. Electronic address: voicescu@icf.ro.
authors.forename: Mariana
authors.initials: M
authors.lastname: Voicescu
authors.affiliation: Romanian Academy, Institute of Physical Chemistry "Ilie Murgulescu", Splaiul Independentei 202, 060021 Bucharest, Romania.
authors.forename: Rodica
authors.initials: R
authors.lastname: Bandula
mesh_terms: D065966:Absorption, Physicochemical; D000818:Animals; D002417:Cattle; D003505:Cyclodextrins / Q000737:chemistry*; D005419:Flavonoids / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011522:Protons; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013696:Temperature; D014364:Tryptophan / Q000737:chemistry
chemical_list: C555160:3,6-dihydroxyflavone; D003505:Cyclodextrins; D005419:Flavonoids; D011522:Protons; D012710:Serum Albumin, Bovine; D014364:Tryptophan
keywords: Cyclodextrins; ESIPT; Flavones; Fluorescence spectroscopy; Proteins