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A carrier protein called bovine serum albumin (BSA) interaction with proton-pump inhibitor such as lansoprazole (LSE) has been investigated at 295, 303 and 311 K in pH 7.40 by docking and [UV–vis, CD, FT–IR and fluorescence (emission, 3D and synchronous)] spectroscopic studies. Emission fluorescence has suggested LSE BSA complex formation by static quenching with strong binding. This interaction has proceeded by Vander Waals and hydrogen bonding. An observation from competitive site marker and docking experiments has resulted in binding of LSE with BSA transpired at site II, whereas from Förster’s theory a binding distance ( ) was retrieved to be 0.19 Å from LSE to Trp of BSA. Change in conformation, secondary structure and microenvironment of BSA were noticed after LSE interaction. Diminished binding constant in Zn, Na, Fe, Ca and Co ions presence on LSE-BSA interaction was also identified.

biointerface research in applied chemistry

Molecular docking and multitudinous spectroscopic studies to elucidating proton-pump inhibitor a lansoprazole binding interaction with bovine serum albumin