Alzheimer’s Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions
نویسندگان
چکیده
منابع مشابه
Cerebrospinal fluid Aβ40 and Aβ42: Natural course and clinical usefulness.
Amyloid β protein 40 (Aβ40) and 42 (Aβ42), major components of senile plaque amyloids, are physiological peptides present in the brain, cerebrospinal fluid (CSF) and plasma. The levels of CSF Aβ40 and Aβ42(43) show a U-shaped natural course in normal aging. The increase of Aβ42(43) over 60 years of age is inhibited in Alzheimer's disease (AD). This specific alteration of CSF Aβ42(43) correlates...
متن کاملAmyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc01743j
Two main amyloid-β peptides of different length (Aβ40 and Aβ42) are involved in Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and mixed oligomers may contribute to the toxic species. However, little is know about the extent of mixing. To study whether Aβ40 and Aβ42 co-aggregate, we used Fourier transform infrared spectroscopy in combination with 13C-l...
متن کاملCSF Aβ42/Aβ40 and Aβ42/Aβ38 ratios: better diagnostic markers of Alzheimer disease
OBJECTIVE The diagnostic accuracy of cerebrospinal fluid (CSF) biomarkers for Alzheimer's disease (AD) must be improved before widespread clinical use. This study aimed to determine whether CSF Aβ42/Aβ40 and Aβ42/Aβ38 ratios are better diagnostic biomarkers of AD during both predementia and dementia stages in comparison to CSF Aβ42 alone. METHODS The study comprised three different cohorts (n...
متن کاملAmyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.
Effects of amyloid beta (Aβ) peptide Aβ(40) on secondary structures of Aβ(42) are studied by all-atom simulations using the GROMOS96 43a1 force field with explicit water. It is shown that in the presence of Aβ(40) the beta-content of monomer Aβ(42) is reduced. Since the fibril-prone conformation N∗ of full-length Aβ peptides has the shape of beta strand-loop-beta strand this result suggests tha...
متن کاملZn2+-Aβ40 complexes form metastable quasi-spherical oligomers that are cytotoxic to cultured hippocampal neurons.
The roles of metal ions in promoting amyloid β-protein (Aβ) oligomerization associated with Alzheimer disease are increasingly recognized. However, the detailed structures dictating toxicity remain elusive for Aβ oligomers stabilized by metal ions. Here, we show that small Zn(2+)-bound Aβ1-40 (Zn(2+)-Aβ40) oligomers formed in cell culture medium exhibit quasi-spherical structures similar to nat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2021
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2020.11.092