Document Type : Regular Article
Department of Chemistry, Bandar Abbas Branch, Islamic Azad University, Bandar Abbas 7915893144, Iran
The binding of ciprofloxacin (CIP) to bovine serum albumin (BSA) in the existence and absence of 6-shogaol was investigated by multiple techniques. Fluorescence spectroscopy results indicated that CIP was able to be quenching of BSA without and with 6-shogaol by way of a static mechanism. The CIP and 6-shogaol binding to BSA leads to the increase of the binding constant (Ka) value of CIP to BSA. In accordance with the minus amounts of ΔH0 and ΔS0, the functions of hydrogen bond and van der Waals forces are very important all over this special binding. In addition, the minus amounts of ΔH0 and ΔS0 for BSA-CIP in the existence of 6-shogaol have been larger than those of the absence of 6-shogaol, which illustrates the higher importance of hydrogen bonding and van der Waals forces. As indicated by the synchronized fluorescence spectroscopy at Δλ = 60 nm, the location of CIP with mixed BSA in binary and trinary systems has been nearer to Tyr residues.