IP Library Granted Patent US 9,023,791
Granted Patent B2
US 9,023,791 · App. 13/296,343 · Granted May 5, 2015

Fibroblast growth factor 21 mutations

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Quick Facts
Patent No.
US 9,023,791
App. No.
13/296,343
Granted
May 5, 2015
Kind
B2
Abstract

The present invention provides novel polypeptide and protein variants of fibroblast growth factor 21 (FGF21) and pharmaceutical compositions comprising FGF21 polypeptide and protein variants.

Claims (44)

1. A polypeptide variant having an amino acid sequence comprising SEQ ID NO:39.

2. The variant of claim 1 , wherein the variant further comprises one or more of the following modifications: (a) an amino-terminal truncation of no more than 5 amino acid residues; and (b) a carboxyl-terminal truncation of no more than 12 amino acid residues.

3. The variant of claim 1 , wherein the variant is covalently linked to polyethylene glycol (PEG) or polysialic acid.

4. The variant of claim 3 , wherein the polyethylene glycol (PEG) or polysialic acid comprises a branched, 40 kDa polyethylene glycol (PEG) or polysialic acid, and wherein said polyethylene glycol (PEG) or polysialic acid is covalently linked to a cysteine of the variant.

5. The variant of claim 3 , wherein the PEG is attached to the cysteine residue at position 122 of SEQ ID NO:39.

6. The variant of claim 5 , wherein the variant further comprises a branched, 40 kDa PEG group at position 122 of SEQ ID NO:39.

7. The variant of claim 1 , wherein the variant is fused to a heterologous protein consisting of one of the following: an IgG constant domain or fragment thereof; Human Serum Albumin (HSA); and an albumin-binding polypeptides.

8. The variant of claim 7 , wherein the heterologous protein is fused to the amino terminus of the variant.

9. The variant of claim 7 , wherein the heterologous protein is fused to the carboxy terminus of the variant.

10. A multimer consisting of the variant of claim 1 .

11. The multimer of claim 10 , wherein the multimer is a homodimer.

12. A pharmaceutical composition comprising the variant of SEQ ID NO:39.

13. The pharmaceutical composition of claim 12 , wherein the variant has a PEG group attached at the cysteine residue at position 122 of SEQ ID NO:39.

14. A polypeptide variant having an amino acid sequence selected from the group consisting of SEQ ID NO:16-19, 38, or 39.

15. The variant of claim 14 , wherein the variant further comprises one or more of the following modifications: (a) an amino-terminal truncation of no more than 5 amino acid residues; and (b) a carboxyl-terminal truncation of no more than 12 amino acid residues.

16. The variant of claim 14 , wherein the variant is covalently linked to polyethylene glycol (PEG) or polysialic acid.

17. The variant of claim 16 , wherein the polyethylene glycol (PEG) or polysialic acid comprises a branched, 40 kDa polyethylene glycol (PEG) or polysialic acid, and wherein said polyethylene glycol (PEG) or polysialic acid is covalently linked to a cysteine of the variant.

18. The variant of claim 16 , wherein the PEG is attached to the cysteine residue at position 122 of SEQ ID NO:39.

19. The variant of claim 18 , wherein the variant further comprises a branched, 40 kDa PEG group at position 122 of SEQ ID NO:39.

20. The variant of claim 14 , wherein the variant is fused to a heterologous protein consisting of one of the following: an IgG constant domain or fragment thereof; Human Serum Albumin (HSA); and an albumin-binding polypeptide.

21. The variant of claim 20 , wherein the heterologous protein is fused to the amino terminus of the variant.

22. The variant of claim 20 , wherein the heterologous protein is fused to the carboxy terminus of the variant.

23. A multimer consisting of at least one of the variants of claim 14 .

24. The multimer of claim 23 , wherein the multimer is a homodimer.

25. A pharmaceutical composition comprising a variant having a sequence selected from the group consisting of SEQ ID NO:16-19, 38, and 39.

26. The pharmaceutical composition of claim 25 , wherein the variant has a PEG group attached at the cysteine residue at position 122 of SEQ ID NO:39.

27. A polypeptide variant comprising a 4 amino acid N-terminally truncated mature FGF21 wild-type protein with the following substitutions made relative to SEQ ID NO:1: a glutamic acid residue substitution at position 56, a histidine residue substitution at position 74, a lysine residue substitution at position 105, an arginine residue substitution at position 150, a glutamine residue substitution at position 159, an alanine residue substitution at position 195, and one or more amino acid substitution that is:

(a) a glutamic acid residue substitution at position 82;

(b) an alanine residue substitution at position 98;

(c) an asparagine residue substitution or a glutamic acid substitution at position 130;

(d) a cysteine residue substitution at position 154; or

(e) a proline residue substitution at position 174.

28. The variant of claim 27 , wherein the variant further comprises one or more of the following modifications: (a) an amino-terminal truncation of no more than 5 amino acid residues; and (b) a carboxyl-terminal truncation of no more than 12 amino acid residues.

29. The variant of claim 27 , wherein the variant is covalently linked to polyethylene glycol (PEG) or polysialic acid.

30. The variant of claim 29 , wherein the polyethylene glycol (PEG) or polysialic acid comprises a branched, 40 kDa polyethylene glycol (PEG) or polysialic acid, and wherein said polyethylene glycol (PEG) or polysialic acid is covalently linked to a cysteine of the variant.

31. The variant of claim 27 , wherein the variant is fused to a heterologous protein consisting of one of the following: an IgG constant domain or fragment thereof; Human Serum Albumin (HSA); and an albumin-binding polypeptides.

32. The variant of claim 31 , wherein the heterologous protein is fused to the amino terminus of the variant.

33. The variant of claim 31 , wherein the heterologous protein is fused to the carboxy terminus of the variant.

34. A multimer consisting of at least one of the variants of claim 27 .

35. The multimer of claim 34 , wherein the multimer is a homodimer.

36. A variant of claim 27 having the cysteine residue substitution at position 122 of SEQ ID NO:39, wherein the variant is covalently linked to polyethylene glycol (PEG) or polysialic acid attached to said cysteine residue.

37. The variant of claim 36 , wherein the variant further comprises a branched, 40 kDa PEG group at position 122 of SEQ ID NO:39.

38. A pharmaceutical composition comprising the variant of claim 27 .

39. A pharmaceutical composition comprising the variant of claim 27 having the cysteine residue substitution at position 122 of SEQ ID NO:39, wherein the variant is covalently linked to polyethylene glycol (PEG) or polysialic acid attached to said cysteine residue.

Assignments (6)
MERGER Recorded Apr 22, 2015
From: IRM LLC
To: NOVARTIS INTERNATIONAL PHARMACEUTICAL LTD.
Reel/Frame 035469/0260 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Apr 22, 2015
From: NOVARTIS INTERNATIONAL PHARMACEUTICAL LTD.
To: NOVARTIS AG
Reel/Frame 035469/0858 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 16, 2012
From: BOETTCHER, BRIAN R.; CAPLAN, SHARI L.; DANIELS, DOUGLAS S.; HAMAMATSU, NORIO; LICHT, STUART; LOEW, ANDREAS; WELDON, STEPHEN CRAIG
To: NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH, INC.
Reel/Frame 027537/0477 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 16, 2012
From: NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH, INC.
To: NOVARTIS AG
Reel/Frame 027537/0511 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 16, 2012
From: GEIERSTANGER, BERNHARD H.
To: NOVARTIS INSTITUTE FOR FUNCTIONAL GENOMICS, INC. D/B/A GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION (GNF)
Reel/Frame 027537/0613 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jan 16, 2012
From: NOVARTIS INSTITUTE FOR FUNCTIONAL GENOMICS, INC. D/B/A GENOMICS INSTITUTE OF THE NOVARTIS RESEARCH FOUNDATION (GNF)
To: IRM LLC
Reel/Frame 027537/0663 →