Neuroprotective agents derived from spider venom peptides
AssigneesThe University of Queensland, Monash University
InventorsGlenn Frederick King, Lachlan Douglas Rash, Irene Chassagnon, Sandy Steffany Pineda Gonzalez, Robert Edward Widdop, Claudia Ann Ireland
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Abstract
The invention relates to disulfide-rich peptides derived from spider venom and their use, particularly as neuroprotective agents. The invention also relates to nucleic acid molecules encoding the peptides as well as constructs and host cells comprising those nucleic acid molecules.
Claims20
An isolated, synthetic, or recombinant peptide, wherein the peptide comprises an amino acid sequence consisting of an N terminal serine residue and any one of SEQ ID NOs:
- 18, 19, and 20.
An isolated, synthetic, or recombinant peptide, wherein the peptide consists of
- a) an amino acid sequence consisting of an N terminal serine residue and any one of SEQ ID NOs:
- 18, 19, and 20, or
- b) SEQ ID NO:
- 19.
A method for treatment of a disease or condition in a subject, wherein the disease or condition is caused by ASIC1a activity or contributed by ASIC1a activity, the method comprising:
- administering a therapeutically effective amount of at least one isolated, synthetic, or recombinant peptide to the subject, wherein the peptide comprises an amino acid sequence selected from the group consisting of:
- (a) an amino acid sequence consisting of an N terminal serine residue and any one of SEQ ID NOs:
- 18, 19, and 20;
- (b) the amino acid sequence of SEQ ID NO:
- 19;
- (c) an amino acid sequence consisting of an N terminal serine residue and an amino acid sequence that shares at least 90% sequence identity with any one of SEQ ID NOs:
- 18, 19, and 20;
- and
- (d) an amino acid sequence that shares at least 90% sequence identity with SEQ ID NO:
- 19,
- wherein the amino acid sequence comprises six cysteine residues covalently joined in pairs to form three disulfide bonds, such that the amino acid sequence comprises one ICK motif, and wherein said peptide is capable of specifically binding to acid sensing ion channel subtype 1a (ASIC1a).
Dependencies are inferred from the claim text.