title: Time-resolved fluorescence study during denaturation and renaturation of curcumin-myoglobin complex.
abstract: Curcumin influences the transition point, the concentration of denaturant required to effect 50% of the total change, of myoglobin denaturation. Curcumin enhances absorbance of myoglobin at 280 nm with a binding constant K=3.0×10(4) M(-1) whereas fluorescence of curcumin is quenched by myoglobin with a Stern-Volmer association constant of 2.5×10(5) M(-1). Unfolding process of myoglobin-curcumin induces a recovery in fluorescence lifetime loss. The gain in time-resolved fluorescence lifetime during unfolding has been again lost during refolding of curcumin-myoglobin complex by dilution process suggesting partial reversibility of unfolding process for both myoglobin and curcumin-myoglobin complex.
authors.affiliation: Department of Chemistry, American University of Beirut, Beirut, Lebanon. dp03@aub.edu.lb
authors.forename: Digambara
authors.initials: D
authors.lastname: Patra
authors.forename: Christelle
authors.initials: C
authors.lastname: Barakat
mesh_terms: D000818:Animals; D003474:Curcumin / Q000378:metabolism* / Q000494:pharmacology*; D004305:Dose-Response Relationship, Drug; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism*; D011489:Protein Denaturation / Q000187:drug effects*; D020673:Protein Renaturation / Q000187:drug effects*; D013050:Spectrometry, Fluorescence; D013997:Time Factors; D014508:Urea / Q000494:pharmacology
chemical_list: D009211:Myoglobin; D014508:Urea; D003474:Curcumin