IP Library Granted Patent US 8,168,754
Granted Patent B2
US 8,168,754 · App. 12/877,553 · Granted May 1, 2012

Modified vitamin K-dependent polypeptides

Assignee: Regents of the University of Minnesota
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Quick Facts
Patent No.
US 8,168,754
App. No.
12/877,553
Granted
May 1, 2012
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 (36)

1. A recombinant vitamin K-dependent polypeptide comprising a modified gamma-carboxyglutamic acid (GLA) domain that enhances membrane binding affinity of said polypeptide compared to a native vitamin K-dependent polypeptide, wherein said modified GLA domain comprises an amino acid insertion at the position corresponding to position 4 of SEQ ID NO:5.

2. The polypeptide of claim 1 , wherein a tyrosine residue is inserted at position 4 of SEQ ID NO:5.

3. The polypeptide of claim 1 , wherein said modified GLA domain further comprises substitution of a hydrophobic amino acid residue or a glutamic acid residue at the position corresponding to position 35 of SEQ ID NO:5.

4. The polypeptide of claim 3 , wherein said hydrophobic amino acid residue is a phenylalanine, leucine or isoleucine residue.

5. The polypeptide of claim 1 , wherein said modified GLA domain further comprises an amino acid substitution at the position corresponding to position 11 of SEQ ID NO:5.

6. The polypeptide of claim 5 , wherein a glutamine, a glutamic acid, an aspartic acid, or an asparagine residue is substituted at position 11 of SEQ ID NO:5.

7. The polypeptide of claim 6 , wherein a glutamine residue is substituted at position 11 of SEQ ID NO:5.

8. The polypeptide of claim 1 , wherein said modified GLA domain further comprises an amino acid substitution at the position corresponding to position 33 of SEQ ID NO:5.

9. The polypeptide of claim 8 , wherein a glutamic acid residue is substituted at position 33 of SEQ ID NO:5.

10. The polypeptide of claim 1 , wherein said modified GLA domain further comprises an amino acid substitution at the position corresponding to position 34 of SEQ ID NO:5.

11. The polypeptide of claim 10 , wherein a hydrophobic residue is substituted at position 34 of SEQ ID NO:5.

12. The polypeptide of claim 11 , wherein a phenylalanine, leucine or isoleucine residue is substituted at position 34 of SEQ ID NO:5.

13. The polypeptide of claim 12 , wherein a phenylalanine residue is substituted at position 34 of SEQ ID NO:5.

14. The polypeptide of claim 1 , wherein said modified GLA domain further comprises an amino acid substitution at the position corresponding to position 29 of SEQ ID NO:5.

15. The polypeptide of claim 14 , wherein a phenylalanine or a glutamic acid residue is substituted at position 29 of SEQ ID NO:5.

16. The polypeptide of claim 15 , wherein a phenylalanine residue is substituted at position 29 of SEQ ID NO:5.

17. A pharmaceutical composition comprising the polypeptide of claim 1 and a pharmaceutically acceptable carrier.

18. A method of increasing clot formation in a mammal, comprising administering an amount of the polypeptide of claim 1 effective to increase clot formation in said mammal.

19. A recombinant Factor VII or Factor VIIa polypeptide comprising a modified GLA domain that enhances membrane binding affinity of said polypeptide compared to a native Factor VII or Factor VIIa polypeptide, wherein said modified GLA domain comprises an amino acid insertion at position 4 of SEQ ID NO:3.

20. The polypeptide of claim 19 , wherein a tyrosine residue is inserted at position 4 of SEQ ID NO:3.

21. The polypeptide of claim 19 , wherein said modified GLA domain further comprises substitution of a hydrophobic amino acid residue or a glutamic acid residue at position 34 of SEQ ID NO:3.

22. The polypeptide of claim 21 , wherein said hydrophobic amino acid residue is a phenylalanine, leucine or isoleucine residue.

23. The polypeptide of claim 19 , wherein said modified GLA domain further comprises an amino acid substitution at position 10 of SEQ ID NO:3.

24. The polypeptide of claim 23 , wherein a glutamine, a glutamic acid, an aspartic acid, or an asparagine residue is substituted at position 10 of SEQ ID NO:3.

25. The polypeptide of claim 24 , wherein a glutamine residue is substituted at position 10 of SEQ ID NO:3.

26. The polypeptide of claim 19 , wherein said modified GLA domain further comprises an amino acid substitution at position 32 of SEQ ID NO:3.

27. The polypeptide of claim 26 , wherein a glutamic acid residue is substituted at position 32 of SEQ ID NO:3.

28. The polypeptide of claim 19 , wherein said modified GLA domain further comprises an amino acid substitution at position 33 of SEQ ID NO:3.

29. The polypeptide of claim 28 , wherein a hydrophobic residue is substituted at position 33 of SEQ ID NO:3.

30. The polypeptide of claim 19 , wherein a phenylalanine, leucine or isoleucine residue is substituted at position 33 of SEQ ID NO:3.

31. The polypeptide of claim 19 , wherein a phenylalanine residue is substituted at position 33 of SEQ ID NO:3.

32. The polypeptide of claim 19 , wherein said modified GLA domain further comprises an amino acid substitution at position 28 of SEQ ID NO:3.

33. The polypeptide of claim 32 , wherein a phenylalanine or a glutamic acid residue is substituted at position 28 of SEQ ID NO:3.

34. The polypeptide of claim 33 , wherein a phenylalanine residue is substituted at position 28 of SEQ ID NO:3.

35. A pharmaceutical composition comprising the polypeptide of claim 19 and a pharmaceutically acceptable carrier.

36. A method of increasing clot formation in a mammal, comprising administering an amount of the polypeptide of claim 19 effective to increase clot formation in said mammal.

Assignments (2)
CONFIRMATORY LICENSE Recorded May 18, 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 035706/0947 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 7, 2010
From: NELSESTUEN, GARY L.
To: REGENTS OF THE UNIVERSITY OF MINNESOTA
Reel/Frame 025459/0534 →
Continuity (3)
Continuation 11377620 · Mar 16, 2006
Continuation 10031005
Related Publication 20110027258A1 · Feb 3, 2011