IP Library Granted Patent US 7,368,432
Granted Patent B2
US 7,368,432 · App. 10/893,300 · Granted May 6, 2008

Conotoxin peptides

Assignees: Xenome, Ltd.; Cognetix, Inc.
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Quick Facts
Patent No.
US 7,368,432
App. No.
10/893,300
Granted
May 6, 2008
Kind
B2
Abstract

The invention relates to relatively short conotoxin peptides, about 10-20 residues in length as described herein, which are naturally available in minute amounts in the venom of the cone snails or analogous to the naturally available peptides, and which preferably include two disulfide bonds. These conotoxin peptides have analgesic activity and are thus useful for treating or preventing pain.

Claims (21)

1. An isolated conotoxin peptide having the amino acid sequence

Ala-Cys-Cys-Gly-Xaa 1 -Xaa 2 -Leu-Cys-Ser-Xaa 3 -Cys (SEQ ID NO :5);

wherein Xaa 1 is Tyr, mono-halo-Tyr, di-halo-Tyr, O-sulpho-Tyr, 0-phospho-Tyr, nitro-Tyr; Xaa 2 is Lys, N-methy-Lys, N,N-dimethyl-Lys or N,N,N-trimethyl-Lys; Xaa 3 is Pro or hydroxy-Pro; and the C-terminus contains a carboxyl or amide group.

2. The isolated conotoxin peptide of claim 1 , wherein Xaa 1 is Tyr.

3. The isolated conotoxin peptide of claim 1 , wherein Xaa 2 is Lys.

4. The isolated conotoxin peptide of claim 1 , wherein Xaa 3 is hydroxy-Pro.

5. The isolated conotoxin peptide of claim 1 , wherein Xaa 1 is Tyr, Xaa 2 is Lys, and Xaa 3 is hydroxy-Pro.

6. The isolated conotoxin peptide of claim 1 , wherein halo is iodine.

7. The isolated conotoxin peptide of claim 6 , wherein Xaa 1 is mono-iodo-Tyr.

8. The isolated conotoxin peptide of claim 6 , wherein Xaa 1 is di-iodo-Tyr.

9. An isolated conotoxin peptide derivative comprising a derivative of the conotoxin peptide of claim 1 , wherein the Xaa2 residue may be substituted with Arg, ornithine, homoarginine, nor-Lys, or a non-natural basic amino acid, wherein the non-natural basic amino acid is selected from the group consisting of N-1-(2-pyrazolinyl)-Arg, 2-(4-piperinyl)-Gly, 2-(4-piperinyl)-Ala, 2-[3-(2S)pyrrolininyl)-Gly and 2-[3-(2S)pyrrolininyl)-Ala; a Tyr residue may be substituted with a 3-hydroxyl or 2-hydroxyl isomer of Tyr or a corresponding O-sulpho- or O-phospho-derivative; a Ser residue may be substituted with a glycosylated Ser; the Cys residues may be in D or L configuration or may be substituted with homocysteine in the D or L configuration.

10. An isolated conotoxin propeptide having the amino acid sequence set forth in SEQ ID NO: 14.

11. The isolated conotoxin peptide of claim 1 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

12. The isolated conotoxin peptide of claim 2 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

13. The isolated conotoxin peptide of claim 3 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

14. The isolated conotoxin peptide of claim 3 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

15. The isolated conotoxin peptide of claim , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

16. The isolated conotoxin peptide of claim 6 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

17. The isolated conotoxin peptide of claim 7 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

18. The isolated conotoxin peptide of claim 8 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

19. The isolated conotoxin peptide of claim 9 , wherein the disulfide bonding is a disulfide bond between the cysteines at amino acid positions 2 and 11 and a disulfide bond between the cysteines at amino acid positions 3 and 8 of SEQ NO:5.

Assignments (2)
CONFIRMATORY LICENSE Recorded Jul 6, 2016
From: UNIVERSITY OF UTAH
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 039264/0709 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 30, 2007
From: UNIVERSITY OF UTAH RESEARCH FOUNDATION
To: XENOME, LTD.
Reel/Frame 019620/0068 →
Continuity (5)
Division 0958020100 · May 26, 2000
Continuation In Part 0949314300 · Jan 28, 2000
Provisional Application 6017329800 · Dec 28, 1999
Provisional Application 6011838100 · Jan 29, 1999
Related Publication 20050143560A1 · Jun 30, 2005