IP Library › Granted Patent US 7,528,108
Granted Patent B2
US 7,528,108 · App. 11/411,603 · Granted May 5, 2009

Compositions and methods for treating or preventing overweight or obesity with zinc-charged protein fragments

Assignee: Ambryx Biotechnology, Inc.
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Quick Facts
Patent No.
US 7,528,108
App. No.
11/411,603
Granted
May 5, 2009
Kind
B2
Abstract

Compositions and methods for treating or preventing, for example, overweight or obesity are provided. Compositions provided comprise zinc-charged, protease digested serum or milk proteins. Compositions are administered in a therapeutically effective amount to treat or prevent, for example, overweight or obesity.

Claims (33)

1. A method of treating obesity in a subject in need thereof comprising the step of administering to the subject a composition comprising an effective amount of a zinc-charged, protease-digested protein and an acceptable carrier, excipient or diluent, wherein the protein is zinc-charged by removing bound ions from the protein by contacting the protein with an effective amount of a chelating agent sufficient to remove the bound ions, followed by contacting the protein with a sufficient amount of zinc ion, wherein the protein is selected from the group consisting of α-2-HS-glycoprotein (AHSG), α-1-acid glycoprotein (AAG), α-1-antitrypsin (AAT), albumin, transferrin and alpha fetoprotein, and wherein the zinc-charged, protease-digested protein induces apoptosis of an adipocyte.

2. The method of claim 1 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is at least 0.02 mg/kg of subject's body weight.

3. The method of claim 1 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is up to 4 mg/kg of subject's body weight.

4. The method of claim 1 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 0.02 mg/kg and about 4 mg/kg of subject's body weight.

5. The method of claim 1 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 1 mg per day and about 400 mg per day.

6. The method of claim 1 , wherein the composition comprises two protease-digested, zinc-charged proteins selected from α-2-HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

7. The method of claim 1 , wherein the composition comprises three protease-digested, zinc-charged proteins selected from α-2-HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

8. The method of claim 1 , wherein the protease-digested, zinc-charged protein is less than 10 kilodaltons.

9. The method of claim 1 , wherein the protease-digested, zinc-charged protein is less than 3 kilodaltons.

10. The method of claim 1 , wherein the composition comprises protein fragments substantially of a size less than 10 kilodaltons.

11. The method of claim 1 , wherein the composition comprises protein fragments substantially of a size less than 3 kilodaltons.

12. A method of reducing weight gain or inducing weight loss in a subject in need thereof comprising the step of administering to the subject a composition comprising an effective amount of a zinc-charged, protease-digested protein and an acceptable carrier, excipient or diluent, wherein the protein is zinc-charged by removing bound ions from the protein by contacting the protein with an effective amount of a chelating agent sufficient to remove the bound ions, followed by contacting the protein with a sufficient amount of zinc ion, wherein the protein is selected from the group consisting of α-2-HS-glycoprotein (AHSG), α-1-acid glycoprotein (AAG), α-1-antitrypsin (AAT), albumin, transferrin and alpha fetoprotein, and wherein the zinc-charged, protease-digested protein induces apoptosis of an adipocyte.

13. The method of claim 12 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is at least 0.02 mg/kg of subject's body weight.

14. The method of claim 12 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is up to 4 mg/kg of subject's body weight.

15. The method of claim 12 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 0.02 mg/kg and about 4 mg/kg of subject's body weight.

16. The method of claim 12 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 1 mg per day and about 400 mg per day.

17. The method of claim 12 , wherein the composition comprises two protease-digested, zinc-charged proteins selected from α-2-HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

18. The method of claim 12 , wherein the composition comprises three protease-digested, zinc-charged proteins selected from α-2-HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

19. The method of claim 12 , wherein the protease-digested, zinc-charged protein is less than 10 kilodaltons.

20. The method of claim 12 , wherein the protease-digested, zinc-charged protein is less than 3 kilodaltons.

21. The method of claim 12 , wherein the composition comprises protein fragments substantially of a size less than 10 kilodaltons.

22. The method of claim 12 , wherein the composition comprises protein fragments substantially of a size less than 3 kilodaltons.

23. A method of treating overweight in a subject in need thereof comprising the step of administering to the subject a composition comprising an effective amount of a zinc-charged, protease-digested protein and an acceptable carrier, excipient or diluent, wherein the protein is zinc-charged by removing bound ions from the protein by contacting the protein with an effective amount of a chelating agent sufficient to remove the bound ions, followed by contacting the protein with a sufficient amount of zinc ion, wherein the protein is selected from the group consisting of α-2-HS-glycoprotein (AHSG), α-1-acid glycoprotein (AAG), α-1-antitrypsin (AAT), albumin, transferrin and alpha fetoprotein, and wherein the zinc-charged, protease-digested protein induces apoptosis of an adipocyte.

24. The method of claim 23 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is at least 0.02 mg/kg of subject's body weight.

25. The method of claim 23 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is up to 4 mg/kg of subject's body weight.

26. The method of claim 23 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 0.02 mg/kg and about 4 mg/kg of subject's body weight.

27. The method of claim 23 , wherein said subject is a human and said effective amount of the zinc-charged, protease digested protein is between 1 mg per day and about 400 mg per day.

28. The method of claim 23 , wherein the composition comprises two protease-digested, zinc-charged proteins selected from α-2-HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

29. The method of claim 23 , wherein the composition comprises three protease-digested, zinc-charged proteins selected from α-2HS-glycoprotein, α-1-acid glycoprotein, α-1-antitrypsin, albumin, transferrin and α-fetoprotein.

30. The method of claim 23 , wherein the protease-digested, zinc-charged protein is less than 10 kilodaltons.

31. The method of claim 23 , wherein the protease-digested, zinc-charged protein is less than 3 kilodaltons.

32. The method of claim 23 , wherein the composition comprises protein fragments substantially of a size less than 10 kilodaltons.

33. The method of claim 23 , wherein the composition comprises protein fragments substantially of a size less than 3 kilodaltons.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 7, 2006
From: MEN HWEI TSAI, DAVID
To: AMBRYX BIOTECHNOLOGY, INC.
Reel/Frame 017893/0230 →
Continuity (3)
Continuation In Part 1131581000 · Dec 22, 2005
Continuation In Part 1111479200 · Apr 26, 2005
Related Publication 20070004617A1 · Jan 4, 2007