Effect of sucrose on formation of the beta-amyloid fibrils and D-aspartic acids in Abeta 1-42.
Beta-amyloid peptide 1-42 is a major peptide constituent of beta-amyloid fibrils. We investigated the role of sucrose on the deposition and the D-aspartic acid formation in an amyloidogenic peptide 1-42 under physiological conditions. From analyses using thioflavine-T fluorometric assay and electronmicroscopic spectroscopy after 60 h incubation at 37 degrees C, it was found that sucrose retarded the fibril formation in the amyloidogenic peptide. The retardation of the formation of amyloid fibrils by sucrose was suggested to be not due to viscosity but due to disturbance of the assemlby of alpha-helix containing peptides. Moreover, we showed that the formation of D-aspartyl residue, which is found in beta-amyloid fibrils from Alzheimer disease brains, in the amyloidogenic peptide was also retarded in the presence of sucrose.
Ueda
Tadashi
T
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan. ueda@phar.kyushu-u.ac.jp
Nagata
Makiko
M
Monji
Akira
A
Yoshida
Ichiro
I
Tashiro
Nobutada
N
Imoto
Taiji
T
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D001224:Aspartic Acid / Q000378:metabolism*; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000737:chemistry*; D013395:Sucrose / Q000494:pharmacology*
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42); D001224:Aspartic Acid; D013395:Sucrose