IP Library Granted Patent US 7,897,404
Granted Patent B2
US 7,897,404 · App. 10/381,941 · Granted Mar 1, 2011

Conjugates of defined stoichiometry

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Quick Facts
Patent No.
US 7,897,404
App. No.
10/381,941
Granted
Mar 1, 2011
Kind
B2
Abstract

The invention relates to a process for the production of a biomolecule-linker conjugate of uniform stochiometry. It especially relates to a conjugate consisting of a biomolecule of a molecular weight between 5 kD and 500 kD and a hydrophilic linker molecule said linker having a molecular weight between 1 and 15 kD and between 4 and 60 charged residues, characterized in that said conjugate comprises at least one biomolecule-linker product of uniform stoichiometry in a pre-selected amount.

Claims (20)

1. A process for production of a fraction of conjugates, each conjugate comprising a biomolecule and a linker and having a pre-defined ratio of biomolecule to linker so that the fraction has a pre-determined and uniform stoichiometry with respect to biomolecule and linker,

wherein the biomolecule has at least two reactive sites, is selected from the group consisting of polypeptides, polysaccharides, and lipopolysaccharides, and, has a molecular weight of between 5 kD and 500 kD, and

wherein the linker is a hydrophilic linker having a molecular weight between 1 kD and 15 kD and containing between 4 and 60 charged residues,

the process comprising:

covalently coupling the biomolecule to the linker, thereby generating a mixture of coupling products comprising the conjugates having the pre-defined ratio of biomolecule to linker,

fractionating by chromatography the mixture of coupling products, and

collecting a fraction comprising the conjugates having the pre-defined ratio of biomolecule to linker, wherein said pre-defined ratio of biomolecule to linker is selected from the group consisting of 1:1, 1:2, 1:3, and 1:4.

2. The process of claim 1 wherein the charged residues are negatively charged.

3. The process of claim 1 wherein the charged residues are positively charged.

4. The process of claim 1 wherein the hydrophilic linker comprises 6 to 50 charged residues.

5. The process of claim 1 wherein the linker comprises a peptide backbone.

6. The process of claim 1 wherein the biomolecule is a polypeptide.

7. The process of claim 1 wherein the chromatographic fractionation is based on differences in apparent molecular weight of the coupling products.

8. The process of claim 7 wherein the linker has an apparent molecular weight between 20% and 500% of that of the biomolecule as determined using molecular sieve chromatography.

9. The process of claim 1 wherein the chromatographic fractionation is based on differences in charge of the coupling products.

10. The process of claim 1 wherein the pre-defined ratio of biomolecule to linker is 1:2.

11. The process of claim 1 wherein the pre-defined ratio of biomolecule to linker is 1:1.

12. The process of claim 1 wherein the linker comprises a β-alanine-glutamic acid peptide.

13. The process of claim 1 wherein the conjugate further comprises a detectable label.

14. The process of claim 1 wherein the conjugate further comprises a member of a bioaffinity binding pair.

Assignments (3)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 3, 2007
From: ROCHE DIAGNOSTICS GMBH, A GERMAN COMPANY
To: ROCHE DIAGNOSTICS CORPORATION
Reel/Frame 019914/0892 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 3, 2007
From: HOESS, EVA; ANDRES, HERBERT; DONIE, FREDERIC; VOGEL, RUDOLF; JOSEL, HANS-PETER; HERRMANN, RUPERT; VON DER ELTZ, HERBERT
To: ROCHE DIAGNOSTICS GMBH, A GERMAN COMPANY
Reel/Frame 019914/0908 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 2, 2004
From: ROCHE DIAGNOSTICS CORPORATION
To: ROCHE DIAGNOSTICS OPERATIONS, INC.
Reel/Frame 015215/0061 →