Abstract
Polysaccharides have attracted great attention for their wide range of applications in biological and medical fields. In this paper, the interaction of polysaccharides with human serum albumin (HSA) was systematically investigated by fluorescence (FL) spectroscopy and circular dichroism (CD) spectra under different conditions. The Stern-Volmer quenching constants (Ka) at different ionic strength and pH were calculated, and information of the structural features of HSA was discussed. FL and CD results indicate that both hydrophobic and electrostatic interactions play important roles during the binding process. The quenching of the fluorescence resulting the binding of polysaccharides and HSA is static.
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