IP Library Granted Patent US 7,812,132
Granted Patent B2
US 7,812,132 · App. 11/377,620 · Granted Oct 12, 2010

Modified vitamin K-dependent polypeptides

Assignee: Regents of the University of Minnesota
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Quick Facts
Patent No.
US 7,812,132
App. No.
11/377,620
Granted
Oct 12, 2010
Kind
B2
Abstract

The invention provides vitamin K-dependent polypeptides with enhanced membrane binding affinity. These polypeptides can be used to modulate clot formation in mammals. Methods of modulating clot formation in mammals are also described.

Claims (34)

1. A recombinant vitamin K-dependent polypeptide comprising a modified GLA domain that enhances membrane binding affinity of said polypeptide relative to a corresponding native vitamin K-dependent polypeptide, said modified GLA domain comprising a hydrophobic amino acid residue substituted at the position corresponding to position 34 of SEQ ID NO:5.

2. The polypeptide of claim 1 , further comprising an amino acid substitution at the position corresponding to position 5, 9, 11, 12, 29, 33, 35, or 36 of SEQ ID NO:5.

3. The polypeptide of claim 1 , further comprising an amino acid substitution at the position corresponding to position 11 of SEQ ID NO:5.

4. The polypeptide of claim 3 , further comprising an amino acid substitution at the position corresponding to position 29 or 33 of SEQ ID NO:5.

5. The polypeptide of claim 4 , wherein a glutamine residue is substituted at the position corresponding to position 11 and a glutamic acid residue is substituted at the position corresponding to position 33 of SEQ ID NO:5.

6. The polypeptide of claim 5 , further comprising an amino acid substitution at the position corresponding to position 35 of SEQ ID NO:5.

7. The polypeptide of claim 6 , wherein a glutamic acid residue is substituted at the position corresponding to position 35 of SEQ ID NO:5.

8. The polypeptide of claim 7 , wherein a phenylalanine, leucine or isoleucine residue is substituted at the position corresponding to position 34 of SEQ ID NO:5.

9. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and an amount of the polypeptide of claim 8 effective to increase clot formation in a mammal.

10. The polypeptide of claim 1 , further comprising an amino acid substitution at the position corresponding to position 35 of SEQ ID NO:5.

11. A recombinant Factor VII or Factor VIIa polypeptide comprising a modified GLA domain that enhances membrane binding affinity of said polypeptide relative to a corresponding native Factor VII or Factor VIIa polypeptide, said modified GLA domain comprising a hydrophobic amino acid residue substituted at position 33 of SEQ ID NO:3.

12. The polypeptide of claim 11 , wherein a phenylalanine, leucine or isoleucine residue is substituted at position 33.

13. The polypeptide of claim 11 , further comprising an amino acid substitution at position 10.

14. The polypeptide of claim 13 , wherein a glutamine, asparagine, glutamic acid, or aspartic acid residue is substituted at position 10.

15. The polypeptide of claim 14 , wherein a glutamine residue is substituted at position 10.

16. The polypeptide of claim 15 , further comprising an amino acid substitution at position 32.

17. The polypeptide of claim 16 , wherein a glutamic acid residue is substituted at position 32.

18. The polypeptide of claim 17 , further comprising an amino acid substitution at position 34.

19. The polypeptide of claim 18 , further comprising an amino acid residue inserted at position 4.

20. The polypeptide of claim 19 , wherein a tyrosine residue is inserted at position 4.

21. The polypeptide of claim 18 , wherein a glutamic acid residue substituted at position 34.

22. The polypeptide of claim 21 , wherein a phenylalanine, leucine or isoleucine residue is substituted at position 33.

23. The polypeptide of claim 22 , wherein a phenylalanine residue is substituted at position 33.

24. A pharmaceutical composition comprising a pharmaceutically acceptable carrier and an amount of a recombinant Factor VII or Factor VIIa polypeptide effective to increase clot formation in a mammal, wherein said Factor VII or Factor VIIa polypeptide comprises a modified GLA domain that enhances membrane binding affinity of said polypeptide relative to a corresponding native Factor VII or Factor VIIa polypeptide, said modified GLA domain comprising a hydrophobic amino acid residue substituted at position 33 of SEQ ID NO:3.

25. The pharmaceutical composition of claim 24 , wherein said polypeptide further comprises an amino acid substitution at position 10, 28, 32, or 34.

26. The pharmaceutical composition of claim 25 , wherein a phenylalanine, leucine or isoleucine residue substituted at position 33.

27. The pharmaceutical composition of claim 26 , said polypeptide further comprising a glutamine residue substituted at position 10.

28. The pharmaceutical composition of claim 27 , said polypeptide further comprising a glutamic acid residue substituted at position 32.

29. The pharmaceutical composition of claim 28 , said polypeptide further comprising an amino acid substitution at position 34.

30. The pharmaceutical composition of claim 29 , said polypeptide further comprising a glutamic acid residue substituted at position 34.

31. The pharmaceutical composition of claim 30 , wherein a phenylalanine residue is substituted at position 33.

32. The pharmaceutical composition of claim 29 , said polypeptide further comprising an amino acid residue inserted at position 4.

33. The pharmaceutical composition of claim 32 , wherein a tyrosine residue is inserted at position 4.

34. The pharmaceutical composition of claim 24 , wherein said pharmaceutical composition further comprises soluble tissue factor.

Assignments (2)
CONFIRMATORY LICENSE Recorded May 12, 2015
From: UNIVERSITY OF MINNESOTA
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 035650/0103 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jun 8, 2010
From: NELSESTUEN, GARY L.
To: REGENTS OF THE UNIVERSITY OF MINNESOTA
Reel/Frame 024499/0414 →
Continuity (2)
Continuation 1003100500
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