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Gel electrophoretic distinction between toxic and nontoxic forms of beta‐amyloid (1—40)
Author(s) -
Brining Sheryl K.,
Chen g,
Yi Daniel,
Chrambach Andreas
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19990601)20:7<1398::aid-elps1398>3.0.co;2-1
Subject(s) - congo red , amyloid (mycology) , chemistry , senile plaques , electrophoresis , beta (programming language) , amyloid beta , polyacrylamide gel electrophoresis , solubility , binding site , alzheimer's disease , biophysics , biochemistry , biology , disease , organic chemistry , enzyme , medicine , pathology , peptide , inorganic chemistry , adsorption , computer science , programming language
The in vitro toxicity of synthetic beta‐amyloid (1—40) correlates with its binding to Congo red (CR). Potentially, therefore, CR binding to the beta‐amyloid containing neuritic plaques in Alzheimer's disease could be used diagnostically. Using polyacrylamide under nondenaturing conditions, the present study shows that both CR binding and nonbinding synthetic beta‐amyloid exhibits multiple charge‐isomeric and size‐isomeric species. The CR binding species exhibit values of free electrophoretic mobility, related to the surface charge density of the protein, which are less than those of the CR nonbinding species within 95% confidence limits. Since surface net charge and solubility are correlated, the decreased solubility of the CR binding species may be responsible for the relative abundance and CR binding of beta‐amyloid in the neuritic plaques of Alzheimer patients.