作者: Hua-xin Zhang , Qun Zhang , Hong-lin Wang , Li-wei Li
DOI: 10.1002/BIO.3285
关键词:
摘要: This study was designed to compare the protein-binding characteristics of aspirin-zinc complex (AZN) with those aspirin itself. AZN synthesized and interacted a model transport protein, human serum albumin (HSA). Three-dimensional fluorescence, ultraviolet-visible circular dichroism (CD) spectra were used characterize interaction HSA under physiological conditions. The mechanism explored using fluorescence quenching method thermodynamic calculation. binding site locality on demonstrated probe technique Forster non-radiation energy transfer theory. Synchronous CD employed reveal effect native conformation protein. HSA-binding results for compared consistent experimental conditions, indicated that acts as guide in when Sudlow's I, subdomain IIA molecule. Moreover, aspirin, showed greater observed constants with, but smaller changes α-helicity of, HSA, which proved might be easier have less toxicity vivo.