Study of the interaction of proteins with curcumin and SDS and its analytical application.
It is found that protein and sodium dodecyl sulphonate (SDS) can enhance resonance light scattering (RLS) of curcumin (CU). Based on this phenomenon, a new quantitative method for protein in aqueous solution has been developed. In the BR (pH 3.5) buffer, the RLS intensity of CU-SDS system is greatly enhanced by protein. The enhanced RLS is proportional to the concentration of protein in the range of 0.00020-20.0 microgml(-1) for bovine serum albumin (BSA) and 0.00040-1.0 microgml(-1) for human serum albumin (HSA) and their detection limits are 0.16 and 0.041 ngml(-1), respectively. An actual sample is satisfactorily determined. In addition, the interaction mechanism between protein and CU-SDS is also studied by using multi-techniques such as RLS, absorption spectroscopy and fluorescence, zeta potential assay measurement.
Wang
Feng
F
Key Lab of Colloid and Interface Chemistry of Education Ministry, School of Chemistry and Chemical Engineering, Shandong University, Jinan 250100, PR China.
Yang
Jinghe
J
Wu
Xia
X
Liu
Shufang
S
D000818:Animals; D002021:Buffers; D002417:Cattle; D003474:Curcumin / Q000737:chemistry* / Q000528:radiation effects; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008027:Light; D012542:Scattering, Radiation; D012709:Serum Albumin / Q000032:analysis* / Q000737:chemistry*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry
D002021:Buffers; D012709:Serum Albumin; D013501:Surface-Active Agents; D012967:Sodium Dodecyl Sulfate; D003474:Curcumin