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A laser light scattering study of the interaction between human serum albumin and ampicillin sodium
Authors:Wang?Weiping,Tang?Jianghong,Peng?Xuhong,Hu?Zhide?  author-information"  >  author-information__contact u-icon-before"  >  mailto:huzd@lzu.edu.cn"   title="  huzd@lzu.edu.cn"   itemprop="  email"   data-track="  click"   data-track-action="  Email author"   data-track-label="  "  >Email author,Chen?Xingguo
Affiliation:Department of Chemistry, Lanzhou University, Lanzhou 730000, China
Abstract:The complexes formed by the interaction of human serum albumin and ampicillin sodium in aqueous solutions were investigated at 25 ± 0.1°C, ionic strength I = 0.085 mol·kg−1, pH 4.9, 5.8 and 7.4. The results of static light scattering have suggested that at pH 7.4, 5.8, 4.9, the molecular weight of the protein/drug complexes is 210,000 g·mol−1, 418,000 g·mol−1, 448,000 g·mol−1, respectively. The z-average root-mean-square radius of gyration and the second virial coefficients decrease with pH decreasing. Dynamic light scattering provides information on diffusion coefficient and particle distributions of protein/drug complexes under different conditions, which suggests a broad hydrodynamic diameter range of scatters. The diffusion coefficients of the systems change with ampicillin sodium concentration and pH changing.
Keywords:human serum albumin (HSA)  ampicillin sodium (AMP)  dynamic light scattering (DLS)  static light scattering (SLS)
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