Article ID Journal Published Year Pages File Type
5371459 Biophysical Chemistry 2011 9 Pages PDF
Abstract
►Distinctive 'two color' fluorescence signatures and fairly high fluorescence anisotropy of fisetin (3,7,3′,4′-OH-flavone) and 3-hydroxyflavone reveal their binding with HbA. ►Specific interactions with HbA are confirmed from the static nature of the flavonoid-induced quenching of protein tryptophan fluorescence. ►Molecular docking and electrostatic surface potential calculations reveal contrasting binding modes of fisetin and 3-hydroxyflavone with HbA.
Related Topics
Physical Sciences and Engineering Chemistry Physical and Theoretical Chemistry
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