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- W3090249314 abstract "Alzheimer's disease (AD) is one of the most devastating neurodegenerative diseases without effective therapies. Immunotherapies using antibodies to lower assembled Aβ provide a promising approach and have been widely studied. Anti-amyloid antibodies are often selective to amyloid conformation, and the lack of amyloid-antibody structural information limits our understanding of these antibodies' conformation selection. Gantenerumab and crenezumab are two anti-Aβ antibodies that bind multiple forms of Aβ with different Aβ epitope preferences. Here, using molecular dynamic (MD) simulations, we study the binding of these two antibodies to the Aβ1-40 fibril, whose conformation is derived from an AD patient's brain tissue. We find that gantenerumab recognizes the Aβ1-11 monomer fragment only at slightly lower pH than the physiological environment where His6 of Aβ1-11 is protonated. Both gantenerumab and crenezumab bind with integrated Aβ fibril rather than binding to monomers within the fibril. Gantenerumab preferentially binds to the N-terminal region of the Aβ1-40 fibril, and the binding is driven by aromatic interactions. Crenezumab can recognize the N-terminal region, as well as the cross-section of the Aβ1-40 fibril, indicating its multiple binding modes in Aβ fibril recognition. These results demonstrate conformation-dependent interactions of antibody-amyloid recognition." @default.
- W3090249314 created "2020-10-08" @default.
- W3090249314 creator A5025357844 @default.
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- W3090249314 date "2020-09-29" @default.
- W3090249314 modified "2023-09-29" @default.
- W3090249314 title "Computational Investigation of Gantenerumab and Crenezumab Recognition of Aβ Fibrils in Alzheimer’s Disease Brain Tissue" @default.
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- W3090249314 doi "https://doi.org/10.1021/acschemneuro.0c00364" @default.
- W3090249314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32991803" @default.
- W3090249314 hasPublicationYear "2020" @default.
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