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Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-?.

ABSTRACT: Bapineuzumab (AAB-001) and its derivative (AAB-003) are humanized versions of the anti-A? murine antibody 3D6 and are immunotherapy candidates in Alzheimer's disease. The common Fab fragment of these immunotherapies has been expressed, purified and crystallized in complex with ?-amyloid peptides (residues 1-8 and 1-28). Diffraction data at high resolution were acquired from crystals of Fab-A?8 (2.0?Å) and Fab-A?28 (2.2?Å) complexes at the Australian Synchrotron. Both crystal forms belonged to the primitive orthorhombic space group P21221.

SUBMITTER: Crespi GA 

PROVIDER: S-EPMC3944706 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of the Fab portion of the Alzheimer's disease immunotherapy candidate bapineuzumab complexed with amyloid-β.

Crespi Gabriela A N GA   Ascher David B DB   Parker Michael W MW   Miles Luke A LA  

Acta crystallographica. Section F, Structural biology communications 20140220 Pt 3

Bapineuzumab (AAB-001) and its derivative (AAB-003) are humanized versions of the anti-Aβ murine antibody 3D6 and are immunotherapy candidates in Alzheimer's disease. The common Fab fragment of these immunotherapies has been expressed, purified and crystallized in complex with β-amyloid peptides (residues 1-8 and 1-28). Diffraction data at high resolution were acquired from crystals of Fab-Aβ8 (2.0 Å) and Fab-Aβ28 (2.2 Å) complexes at the Australian Synchrotron. Both crystal forms belonged to th  ...[more]

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