Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method

Abstract We investigated the interaction between colchicine and bovine serum albumin (BSA) by fluorescence and UV–Vis absorption spectroscopy. In the mechanism discussion, it was proved that the fluorescence quenching of BSA by colchicine is a result of the formation of colchicine–BSA complex; van der Waals interactions and hydrogen bonds play a major role in stabilizing the complex. The modified Stern–Volmer quenching constant K a and corresponding thermodynamic parameters Δ H , Δ G , Δ S at different temperatures were calculated. The distance r between donor (BSA) and acceptor (colchicine) was obtained according to fluorescence resonance energy transfer (FRET).

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