# US 2014/0154774 A1 · Npp1 fusion proteins

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- Number: US 2014/0154774 A1
- Document ID: US20140154774A1
- Status: Published application
- Kind: A1
- Application number: 14/004,294
- Filed: 2011-09-15
- Published: 2014-06-05
- Earliest claimed: 2011-03-11
- Assignees: Synageva BioPharma Corp.
- Inventors: Anthony Quinn; Alex J. Harvey; Zhinan Xia
- Web page: https://patentgrep.com/patent/US20140154774A1

## CPC

- C12N 9/16: acting on ester bonds (3.1)
- A61P 3/10: for hyperglycaemia, e.g. antidiabetics
- A61P 7/00: Drugs for disorders of the blood or the extracellular fluid
- A61P 9/00: Drugs for disorders of the cardiovascular system
- A61P 9/10: for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
- A61P 19/02: for joint disorders, e.g. arthritis, arthrosis
- A61P 19/08: for bone diseases, e.g. rachitism, Paget's disease
- A61P 21/00: Drugs for disorders of the muscular or neuromuscular system
- C07K 7/06: having 5 to 11 amino acids
- C12N 9/00: Enzymes; Proenzymes; Compositions thereof (preparations containing enzymes for cleaning teeth A61K8/66, A61Q11/00; medicinal preparations containing enzymes or proenzymes A61K38/43; enzyme containing detergent compositions C11D; {enzymes with nucleic acid structure, e.g. ribozymes, C12N15/113}); Processes for preparing, activating, inhibiting, separating or purifying enzymes (preparation of malt C12C1/00)
- C12N 9/22: Ribonucleases {[RNase]; Deoxyribonucleases [DNase]}
- C12N 9/96: Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
- C12N 15/625: {containing a sequence coding for a signal sequence}
- C12N 15/8509: {for producing genetically modified animals, e.g. transgenic}
- C12N 15/86: Viral vectors
- C12Y 301/04001: Phosphodiesterase I (3.1.4.1)
- A61K 38/00: Medicinal preparations containing peptides (peptides containing beta-lactam rings A61K31/00; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, A61K31/00; ergot alkaloids of the cyclic peptide type A61K31/48; containing macromolecular compounds having statistically distributed amino acid units A61K31/74; medicinal preparations containing antigens or antibodies A61K39/00; medicinal preparations characterised by the non-active ingredients, e.g. peptides as drug carriers, A61K47/00)
- C07K 2319/00: Fusion polypeptide
- C07K 2319/01: containing a localisation/targetting motif
- C07K 2319/02: containing a signal sequence
- C07K 2319/30: Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
- C07K 2319/33: fusions for targeting to specific cell types, e.g. tissue specific targeting, targeting of a bacterial subspecies
- C12N 2840/007: cell or tissue specific
- Y10S 530/827: Proteins from mammals or birds
- C12N: MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA (microbiological testing media C12Q1/00)
- A61P: SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- C07K: PEPTIDES (peptides in foodstuffs A23; obtaining protein compositions for foodstuffs, working-up proteins for foodstuffs A23J; preparations for medicinal purposes A61K; peptides containing beta-lactam rings C07D; cyclic dipeptides not having in their molecule any other peptide link than those which form their ring, e.g. piperazine-2,5-diones, C07D; ergot alkaloids of the cyclic peptide type C07D519/02; macromolecular compounds having statistically distributed amino acid units in their molecules, i.e. when the preparation does not provide for a specific; but for a random sequence of the amino acid units, homopolyamides and block copolyamides derived from amino acids C08G69/00; macromolecular products derived from proteins C08H1/00; preparation of glue or gelatine C09H; single cell proteins, enzymes C12N; genetic engineering processes for obtaining peptides C12N15/00; compositions for measuring or testing processes involving enzymes C12Q; investigation or analysis of biological material G01N33/00)
- C12Y: ENZYMES
- A61K: PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES (devices or methods specially adapted for bringing pharmaceutical products into particular physical or administering forms A61J3/00; chemical aspects of, or use of materials for deodorisation of air, for disinfection or sterilisation, or for bandages, dressings, absorbent pads or surgical articles A61L; soap compositions C11D)
- Y10S: TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS

## Abstract

The present invention provides a novel fusion polypeptide containing a catalytic domain of NPP1 fused to a targeting moiety, nucleic acids encoding the fusion polypeptide, a vector containing the nucleic acid integrated thereinto, a host cell transformed with the vector and pharmaceutical compositions comprising the fusion polypeptide.

## Claims

### Claim at position 1

1-38. (canceled)

### Claim 39

An isolated polypeptide comprising a targeting moiety and a catalytic domain of NPP1, wherein said catalytic domain of NPP1 comprises the amino acid sequence set forth from P99 to D925 of SEQ ID NO:1.

### Claim 40 (depends on 39)

The polypeptide of claim 39, wherein said targeting moiety is a peptide comprising about five to about eighteen consecutive negatively charged amino acid residues.

### Claim 41 (depends on 39)

The polypeptide of claim 39, wherein said negatively charged amino acid residues are aspartic acid or glutamic acid.

### Claim 42 (depends on 41)

The polypeptide of claim 41, wherein said negatively charged amino acid residues comprise about 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17 or 18 consecutive aspartic acid or glutamic acid residues.

### Claim 43 (depends on 42)

The polypeptide of claim 42, wherein said negatively charged amino acid residues comprise about eight consecutive aspartic acid residues.

### Claim 44 (depends on 42)

The polypeptide of claim 42, wherein said negatively charge amino acid residues comprises about ten consecutive aspartic acid residues.

### Claim 45 (depends on 41)

The polypeptide of claim 41, wherein said negatively charged amino acid residues comprise about 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive aspartic acid residues.

### Claim 46 (depends on 45)

The polypeptide of claim 45, wherein said negatively charged amino acid residues comprise about eight consecutive glutamic acid residues.

### Claim 47 (depends on 45)

The polypeptide of claim 45, wherein said negatively charge amino acid residues comprises about ten consecutive glutamic acid residues.

### Claim 48 (depends on 39)

The polypeptide of claim 39, wherein said targeting moiety is fused to C-terminus of said catalytic domain of NPP1.

### Claim 49 (depends on 42)

The polypeptide of claim 42, wherein said polypeptide further comprises an Fc region of an immunoglobulin.

### Claim 50 (depends on 49)

The polypeptide of claim 49, wherein said Fc region comprises the amino acid sequence set forth in SEQ ID NO:16.

### Claim 51 (depends on 50)

The polypeptide of claim 50, wherein said targeting moiety is ten consecutive aspartic acid residues.

### Claim 52 (depends on 49)

The polypeptide of claim 49, wherein said Fc region is fused to C-terminus of said catalytic domain of NPP1.

### Claim 53 (depends on 39)

The polypeptide of claim 39, wherein said polypeptide further comprises a signal peptide.