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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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14001642

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  1. National Health and Medical Research Council of Australia (NHMRC) [APP1021935]
  2. JO & JR Wicking Trust
  3. Mason Foundation
  4. Bethlehem Griffith Research Foundation
  5. Australian Cancer Research Foundation
  6. Victorian Government
  7. Winston Churchill Memorial Trust

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Bapineuzumab (AAB-001) and its derivative (AAB-003) are humanized versions of the anti-A beta 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 beta-amyloid peptides (residues 1-8 and 1-28). Diffraction data at high resolution were acquired from crystals of Fab-A beta(8) (2.0 angstrom) and Fab-A beta(28) (2.2 angstrom) complexes at the Australian Synchrotron. Both crystal forms belonged to the primitive orthorhombic space group P2(1)22(1).

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