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New Structural View on How Amyloid Beta Production Hints Alzheimer’s Disease Pathology
Xiaodan Yan, Qin Yang, Jenna Howe, QingShan Bill Fu, and Longfei Wang
Harvard University
Departmentof Biological Chemistry and Molecular Pharmacology, Harvard Medical Schoo

The accumulation of amyloid beta (Aβ) peptide faulty isoform has been found to cause Alzheimer’sdisease (AD) as itis the major component of amyloid senile plaques in the extracellular matrix of brains of AD patients. Aβ42 (only two amino acid longer than Aβ40) tends to aggregate, forming neurotoxic oligomers and fibrils. A lot of studies were focused on Aβ42, but all failed explain why the production balance of Aβ42 and Aβ40 leans towards Aβ42 in neurons of Alzheimer’s patients. A recent study, utilizing NMR technology, was able to illustrate the molecular mechanism of abnormal formation of Aβ42. A mutant of the amyloid precursor protein found in familial AD, V44M, was shown to alter the structure of its transmembrane region, leading to the exposure of residueT48. The exposure of T48 leads to the shift of cleavage by γ-secretase from residue L49 to residue T48, thus producing the Aβ42 isoform. In this highlight, we explain the work in detail and discuss its implications on potential treatment of AD.


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