Molecular modeling and spectroscopic studies on the binding of guaiacol to human immunoglobulin

摘要: The fluorogenic property of guaiacol was exploited for the first time to analyze interaction with target protein as a probe by molecular modeling, fluorescence, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. Molecular docking performed reveal possible binding mode or mechanism suggested that can strongly bind human immunoglobulin (HIgG). It is considered binds HIgG mainly hydrophobic there are two hydrogen bond interactions between drug residues LEU 80 ASP 65, which in good agreement results from experimental thermodynamic parameters (the enthalpy change Δ H 0 entropy S were calculated be 65.55 kJ·mol -1 132.95 J·mol ·K according Vant’ Hoff equation). Data obtained fluorescence spectroscopy indicated leads dramatic enhancement emission intensity along significant occurrence efficient Forster resonance energy transfer (FRET) residue bound guaiacol. From low value anisotropy ( r = 0.06), it argued molecule located motionally unrestricted environment protein. alterations protein’s secondary structure presence aqueous solution quantitatively evidences FT-IR CD spectroscopes.