IP Library Granted Patent US 7,816,490
Granted Patent B2
US 7,816,490 · App. 12/260,049 · Granted Oct 19, 2010

Specific inhibitors of NFAT activation by calcineurin and their use in treating immune-related diseases

Assignee: Immune Disease Institute, Inc.
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 7,816,490
App. No.
12/260,049
Granted
Oct 19, 2010
Kind
B2
Abstract

Isolated peptide fragments of the conserved regulatory domain of NFAT protein capable of inhibiting protein-protein interaction between calcineurin and NFAT, or a biologically active analog thereof are described. Isolated polynucleotides and gene therapy vectors encoding such peptide fragments are also described. In addition, methods for treating immune-related diseases or conditions and methods for high throughput screening of candidate agents are described. Pharmaceutical compositions are also provided.

Claims (30)

1. An NFAT derivative comprising the sequence of SEQ ID NO:22, wherein at least one non-conserved residue in SEQ ID NO:22 is substituted, and wherein the NFAT derivative is less than 50 amino acid residues long and binds to calcineurin.

2. The NFAT derivative of claim 1 , wherein the NFAT derivative is less than 20 amino acid residues long.

3. A peptide inhibitor of protein-protein interaction between calcineurin and NFAT identified by a process comprising the steps of:

providing a first compound comprising NFAT or a biologically active derivative thereof;

providing a second compound comprising calcineurin or a biologically active derivative thereof;

providing a candidate agent;

contacting said first compound, said second compound and said candidate agent with each other;

determining the amount of said second compound bound to said first compound or determining the amount of said first compound bound to said second compound, wherein a reduction in binding between said first compound and said second compound indicates that said candidate agent is an inhibitor of protein-protein interaction between calcineurin and NFAT; and

wherein the peptide inhibitor is an NFAT derivative comprising the sequence of SEQ ID NO:22, wherein at least one non-conserved residue in SEQ ID NO:22 is substituted, and wherein the NFAT derivative is less than 150 amino acid residues long and binds to calcineurin.

4. The peptide inhibitor of claim 3 , wherein the NFAT derivative is less than 20 amino acid residues long.

5. An NFAT derivative comprising the sequence of SEQ ID NO:5, wherein at least one non-conserved residue in SEQ ID NO:5 is substituted, and wherein the NFAT derivative is less than 50 amino acid residues long and binds to calcineurin.

6. The NFAT derivative of claim 5 , wherein the NFAT derivative is less than 20 amino acid residues long.

7. The NFAT derivative of claim 5 , wherein the NFAT derivative is less than 10 amino acid residues long.

8. The NFAT derivative of claim 5 , wherein the NFAT derivative is 6 amino acid residues long.

9. A peptide inhibitor of protein-protein interaction between calcineurin and NFAT identified by a process comprising the steps of:

providing a first compound comprising NFAT or a biologically active derivative thereof;

providing a second compound comprising calcineurin or a biologically active derivative thereof;

providing a candidate agent;

contacting said first compound, said second compound and said candidate agent with each other;

determining the amount of said second compound bound to said first compound or determining the amount of said first compound bound to said second compound, wherein a reduction in binding between said first compound and said second compound indicates that said candidate agent is an inhibitor of protein-protein interaction between calcineurin and NFAT; and

wherein the peptide inhibitor is an NFAT derivative comprising the sequence of SEQ ID NO:5, wherein at least one non-conserved residue in SEQ ID NO:5 is substituted, and wherein the NFAT derivative is less than 150 amino acid residues long and binds to calcineurin.

10. The peptide inhibitor of claim 9 , wherein the NFAT derivative is less than 20 amino acid residues long.

11. The peptide inhibitor of claim 9 , wherein the peptide inhibitor is less than 10 amino acid residues long.

12. The peptide inhibitor of claim 9 , wherein the peptide inhibitor is 6 amino acid residues long.

13. The NFAT derivative of claim 1 , wherein the NFAT derivative is 13 amino acid residues long.

14. The peptide inhibitor of claim 3 , wherein the peptide inhibitor is less than 100 amino acid residues long.

15. The peptide inhibitor of claim 3 , wherein the peptide inhibitor is less than 50 amino acid residues long.

16. The peptide inhibitor of claim 3 , wherein the peptide inhibitor is 13 amino acid residues long.

17. The peptide inhibitor of claim 9 , wherein the NFAT derivative is less than 100 amino acid residues long.

18. The peptide inhibitor of claim 9 , wherein the NFAT derivative is less than 50 amino acid residues long.

Assignments (4)
CORRECTIVE ASSIGNMENT TO CORRECT THE NAME OF THE RECEIVING PARTY RECORDED MARCH 27, 2009, FROM THE CENTER FOR BLOOD RESEARCH TO CENTER FOR BLOOD RESEARCH, INC. PREVIOUSLY RECORDED ON REEL 022459 FRAME 0960. ASSIGNOR(S) HEREBY CONFIRMS THE PATRICK G. HOGAN, ANJANA RAO, JOSE ARAMBURU, HEREBY ASSIGN/TRANSFER ALL RIGHTS UNTO CENTER FOR BLOOD RESEARCH, INC.. Recorded Feb 23, 2010
From: HOGAN, PATRICK G.; RAO, ANJANA; ARAMBURU, JOSE
To: CENTER FOR BLOOD RESEARCH, INC.
Reel/Frame 023977/0945 →
CHANGE OF NAME Recorded Dec 11, 2009
From: THE CBR INSTITUTE FOR BIOMEDICAL RESEARCH, INC.
To: IMMUNE DISEASE INSTITUTE, INC.
Reel/Frame 023641/0408 →
CHANGE OF NAME Recorded Apr 1, 2009
From: CENTER FOR BLOOD RESEARCH, INC.
To: THE CBR INSTITUTE FOR BIOMEDICAL RESEARCH, INC.
Reel/Frame 022481/0450 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 27, 2009
From: HOGAN, PATRICK G.; RAO, ANJANA; ARAMBURU, JOSE
To: THE CENTER FOR BLOOD RESEARCH
Reel/Frame 022459/0960 →
Continuity (5)
Division 1147421800 · Jun 23, 2006
Continuation 1006615100 · Jan 31, 2002
Continuation 0924862000 · Feb 11, 1999
Provisional Application 6007446700 · Feb 12, 1998
Related Publication 20090186422A1 · Jul 23, 2009