Human serum albumin interaction with formononetin studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling methods.

摘要: Abstract Interaction of formononetin with a model transport protein, human serum albumin (HSA), has been studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling methods. Upon binding HSA, the spectrum exhibits appreciable hypsochromic shift along an enhancement in intensity. Gradual addition HSA led to marked increase anisotropy ( r ). From value it is argued that drug located restricted environment protein. The constant K  ≈ 1.6 × 10 5  M −1 ) standard free energy change (Δ G 0  ≈ −29.9 kJ/mol) formononetin–HSA interaction have calculated according relevant data. Fourier transform infrared measurements shown secondary structures protein changed by HSA. Computational mapping possible sites revealed molecule be bound large hydrophobic cavity subdomain IIA.