IP Library Granted Patent US 6,962,699
Granted Patent B2
US 6,962,699 · App. 10/454,816 · Granted Nov 8, 2005

Rationally designed polysaccharide lyases derived from chondroitinase B

Assignee: Massachusetts Institute of Technology
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Quick Facts
Patent No.
US 6,962,699
App. No.
10/454,816
Granted
Nov 8, 2005
Kind
B2
Abstract

The invention relates to rationally designed polysaccharide lyases and uses thereof. In particular, the invention relates to modified chondroitinase B. The modified chondroitinase B enzymes of the invention are useful for a variety of purposes, including cleaving and sequencing polysaccharides such as glycosaminoglycans (GAGs) as well as removing polysaccharides from a solution. The invention also includes methods of inhibiting anticoagulant activity, inhibiting angiogenesis, treating cancer, and inhibiting maternal malarial infection.

Claims (23)

1. A modified chondroitinase B having an amino acid sequence of the mature peptide of SEQ ID NO: 2 or conservative substitutions thereof, wherein at least one residue at a position selected from the group consisting of 116, 184, 213, 219, 245, 250, 271, 272, 296, 298, 318, 333, 363 and 364 of SEQ ID NO: 2 has been substituted or deleted.

2. The modified chondroitinase B of claim 1 , having a modified product profile, wherein the modified product profile of the modified chondroitinase B is at least 10% different than a native product profile of a native chondroitinase B.

3. The modified chondroitinase B of claim 2 , wherein the modified chondroitinase B has the amino acid sequence of the mature peptide of SEQ ID NO: 2, wherein at least one amino acid residue has been substituted and wherein the substituted amino acid is at a position selected from the group consisting of 272, 333and 364 of SEQ ID NO: 2.

4. The modified chondroitinase B of claim 1 , having a k cat or K M value for a substrate that is at least 10% different than a native chondroitinase B k cat or K M value.

5. The modified chondroitinase B of claim 4 , wherein the modified chondroitinase B has the amino acid sequence of the mature peptide of SEQ ID NO: 2, wherein at least one amino acid residue has been substituted, and wherein the substituted amino acid is at a position selected from the group consisting of 272, 333, 363 and 364 of SEQ ID NO: 2.

6. A composition comprising a sterile formulation of the modified chondroitinase B of claim 1 and a pharmaceutically acceptable carrier.

7. A method of analyzing a sample of polysaccharides, comprising:

contacting the sample with the modified chondroitinase B of claim 1 and analyzing the sample of polysaccharides.

8. A method of identifying the presence of a particular polysaccharide in a sample, comprising:

contacting the sample with the modified chondroitinase B of claim 1 and identifying the presence of a particular polysaccharide in the sample.

9. A method of determining the purity of a sample of polysaccharides, comprising:

contacting the sample with the modified chondroitinase B of claim 1 and determining the purity of the sample of polysaccharides.

10. A method for determining the composition of a sample of polysaccharides, comprising:

contacting the sample with the modified chondroitinase B of claim 1 and determining the composition of the sample of polysaccharides.

11. An immobilized modified chondroitinase B comprising;

a modified chondroitinase B as in claim 1 , and

a solid support membrane, wherein the modified chondroitinase B is immobilized on the solid support membrane.

12. The modified chondroitinase B of claim 1 , wherein the chondroitinase B is a substantially purified recombinant form.

13. The modified chondroitinase B of claim 2 , wherein the modified chondroitinase B has a modified product profile that is at least 20% different than a native product profile of a native chondroitinase B.

14. The modified chondroitinase B of claim 2 , wherein the modified chondroitinase B has a modified product profile that is at least 50% different than a native product profile of a native chondroitinase B.

15. The modified chondroitinase B of claim 4 , wherein the modified chondroitinase B k cat or K M value is at least 20% different than a native chondroitinase B k cat or K M value.

16. The modified chondroitinase B of claim 4 , wherein the modified chondroitinase B k cat or K M value is at least 50% different than a native chondroitinase B k cat or K M value.

17. The modified chondroitinase B of claim 15 , wherein the substrate is a glycosaminoglycan.

Assignments (2)
CONFIRMATORY LICENSE Recorded Jan 14, 2011
From: MASSACHUSETTS INSTITUTE OF TECHNOLOGY
To: NATIONAL INSTITUTES OF HEALTH (NIH), U.S. DEPT. OF HEALTH AND HUMAN SERVICES (DHHS), U.S. GOVERNMENT
Reel/Frame 025636/0077 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Feb 24, 2004
From: POJASEK, KEVIN; RAMAN, RAHUL; SASISEKHARAN, RAM
To: MASSACHUSETTS INSTITUTE OF TECHNOLOGY
Reel/Frame 015006/0086 →
Continuity (2)
Provisional Application 6038550900 · Jun 3, 2002
Related Publication 20040091472A1 · May 13, 2004