IP Library Granted Patent US 7,820,162
Granted Patent B2
US 7,820,162 · App. 12/100,183 · Granted Oct 26, 2010

Methods for chemically synthesizing immunoglobulin chimeric proteins

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Quick Facts
Patent No.
US 7,820,162
App. No.
12/100,183
Granted
Oct 26, 2010
Kind
B2
Abstract

The invention provides methods of chemically synthesizing chimeric proteins comprising at least a portion of an immunoglobulin constant region and a biologically active molecule.

Claims (21)

1. A method of synthesizing a chimeric monomer-dimer hybrid comprising

a) recombinantly expressing a fusion protein comprising a portion of an immunoglobulin containing an Fc neonatal receptor (FcRn) binding site and a splicing protein capable of forming a thioester intermediate on the C terminus of the portion containing the FcRn binding site;

b) adding a thiol cofactor to the fusion protein of a);

c) adding at least one biologically active molecule having an N terminal cysteine, thereby linking the biologically active molecule with the C terminus of the portion containing the FcRn binding site; and

d) adding a second polypeptide containing an FcRn binding site, thereby forming a chimeric monomer-dimer hybrid;

wherein the biologically active molecular is a polypeptide or a nucleic acid molecule.

2. The method of claim 1 , wherein the splicing protein is intein.

3. The method of claim 1 , wherein the thiol cofactor is 2-mercaptoethanesulfonic acid.

4. The method of claim 1 , wherein the monomer-dimer hybrid is a dimerically linked monomer-dimer hybrid.

5. The method of claim 1 , wherein the biologically active molecule is a polypeptide.

6. The method of claim 1 , wherein the biologically active molecule is a nucleic acid molecule.

7. The method of claim 1 , wherein both the biologically active molecule and the fusion protein are produced recombinantly.

8. The method of claim 1 , wherein at least one of the biologically active molecule and the fusion protein is produced by chemical synthesis.

9. The method of claim 1 , wherein the chimeric protein further comprises a linker.

10. The method of claim 1 , wherein the reaction is performed in solution.

11. The method of claim 1 , wherein the reaction is performed on a solid support.

12. The method of claim 11 , wherein the solid support is a chitin bead.

13. The method of claim 1 , wherein the biologically active molecule is selected from the group consisting of erythropoietin (EPO), interferon, a viral fusion inhibitor, and a clotting factor.

14. The method of claim 1 , wherein the biologically active molecule is EPO.

15. The method of claim 1 , wherein the biologically active molecule is interferon α.

16. The method of claim 1 , wherein the biologically active molecule is interferon β.

Assignments (5)
CHANGE OF NAME Recorded Feb 16, 2017
From: BIOGEN HEMOPHILIA INC.
To: BIOVERATIV THERAPEUTICS INC.
Reel/Frame 041735/0659 →
CHANGE OF ADDRESS Recorded Jul 2, 2015
From: BIOGEN HEMOPHILIA INC.
To: BIOGEN HEMOPHILIA INC.
Reel/Frame 036051/0773 →
CHANGE OF NAME Recorded Apr 30, 2015
From: BIOGEN IDEC HEMOPHILIA INC.
To: BIOGEN HEMOPHILIA INC.
Reel/Frame 035553/0325 →
CHANGE OF NAME Recorded Apr 24, 2014
From: SYNTONIX PHARMACEUTICALS, INC.
To: BIOGEN IDEC HEMOPHILIA INC.
Reel/Frame 032753/0837 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 4, 2009
From: MEZO, ADAM R.; PETERS, ROBERT T.
To: SYNTONIX PHARMACEUTICALS, INC.
Reel/Frame 022340/0055 →