Comparative Investigation on the Interaction of Cefonicid Sodium with Bovine Transferrin and Bovine Serum Albumin by Multi-Spectroscopy

摘要: The reaction mechanisms of cefonicid sodium to bovine serum albumin and transferrin were studied by multi-spectroscopy methods. results demonstrated that new complexes formed between the two proteins, which resulted in a static quenching fluorescence proteins. And numbers binding sites systems approximately equal 1. In system, drug binds with proteins mainly through electrostatic force. It also showed hydrophobic environment around amino acid residues changed, primary for both closer tryptophan residues. Circular dichroism spectroscopy secondary structures changed. values Hill's coefficients indicating there negative co-operativities interaction subsequent ligands addition, studies have was stronger. However, had larger influences on microenvironment transferrin. different will be helpful extracting common features, applying unique characteristic drug-proteins systems.