Amyloid-beta peptide crystal structure
AssigneeCommonwealth Scientific and Industrial Research Organisation
InventorsStewart Douglas Nuttall, Victor Anatolievich Streltsov, Joseph Noozhumurry Varghese, Vidanagamage Chandana Epa
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Abstract
The invention relates provides a novel crystal structure of the fibrillogenic part of amyloid β-peptide (Aβ). More specifically the crystal structure is Aβ-IgNAR and, accordingly the present invention also relates to selecting and/or designing compounds that modulate amyloid β-peptide (Aβ) activity using techniques such as in silico screening and crystal soaking experiments. The invention further relates to compounds and methods for inhibiting interaction between amyloid β-peptide (Aβ) monomers, more particularly, inhibiting or disrupting amyloid β-peptide (Aβ) oligomer formation and toxic activity.
Claims23
An amyloid β-peptide-immunoglobulin new antigen receptor fusion molecule (Aβ-IgNAR molecule) having the amino acid sequence of any one of SEQ ID NOs:
- 15 to 24.
A composition comprising a crystal having the coordinates set forth in Appendix I in space group P32 with cell parameters a=b=79.40, c=84.89 Å, which is produced from the Aβ-IgNAR molecule having the amino acid sequence of SEQ ID NO:2.
An amyloid β-peptide-immunoglobulin new antigen receptor fusion molecule (Aβ-IgNAR molecule) comprising amino acids in the sequence of residues 1-87 of the IgNAR set forth as SEQ ID NO:3 fused to amino acids in the sequence of residues 18-41 set forth as SEQ ID NO:1, the sequence of residues 88-111 set forth as SEQ ID NO:19, the sequence of residues 88-111 set forth as SEQ ID NO:20, the sequence of residues 88-111 set forth as SEQ ID NO:21, the sequence of residues 88-111 set forth as SEQ ID NO:22, the sequence of residues 88-110 set forth as SEQ ID NO:23, or the sequence of residues 88-111 set forth as SEQ ID NO:24.
Dependencies are inferred from the claim text.