A novel method for study of the aggregation of protein induced by metal ion aluminum(III) using resonance Rayleigh scattering technique.
We present a novel method for the study of the aggregation of protein induced by metal ion aluminum(III) using resonance Rayleigh scattering (RRS) technique. In neutral Tris-HCl medium, the effect of this aggregation of protein results in the enhancement of RRS intensity and the relationship between the enhancement of the RRS signal and the Al concentration is nonlinear. On this basis, we established a new method for the determination of the critical induced-aggregation concentrations (C(CIAC)) of metal ion Al(III) inducing the protein aggregation. Our results show that many factors, such as, pH value, anions, salts, temperature and solvents have obvious effects. We also studied the extent of aggregation and structural changes using ultra-violet spectrometry, protein intrinsic fluorescence and circular dichroism to further understand the exact mechanisms of the aggregation characteristics of proteins induced by metal ion Al(III) at the molecular level, to help us to develop effective methods to investigate the toxicity of metal ion Al, and to provide theoretical and quantitative evidences for the development of appropriate treatments for neurodementia such as Parkinson's disease, Alzheimer's disease and dementia related to dialysis.
Long
Xiufen
X
School of Chemistry & Chemical Engineering, Nanjing University, Nanjing 210093, China.
Zhang
Caihua
C
Cheng
Jiongjia
J
Bi
Shuping
S
D000535:Aluminum / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D020836:Protein Structure, Quaternary; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012997:Solvents; D013696:Temperature
D012709:Serum Albumin; D012997:Solvents; D012710:Serum Albumin, Bovine; D000535:Aluminum