# US 11,028,144 B2 · Soluble glycoprotein V for treating thrombotic diseases

> Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt

- Number: US 11,028,144 B2
- Document ID: US11028144B2
- Status: Granted
- Kind: B2
- Application number: 16/065,365
- Filed: 2016-12-23
- Published: 2019-06-06
- Granted: 2021-06-08
- Earliest claimed: 2015-12-23
- Assignees: Julius-Maximilians-UniversitäT WüRzburg
- Applicants: Julius-Maximilians-UniversitäT WüRzburg
- Inventors: Bernhard Nieswandt; Sarah Beck; David Stegner
- Web page: https://patentgrep.com/patent/US11028144B2

## CPC

- C07K 14/70596: {Molecules with a "CD"-designation not provided for elsewhere}
- A61K 38/177: {Receptors; Cell surface antigens; Cell surface determinants}
- A61K 38/38: Albumins
- A61K 38/40: Transferrins, e.g. lactoferrins, ovotransferrins
- A61K 45/06: Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
- A61K 47/60: the organic macromolecular compound being a polyoxyalkylene oligomer, polymer or dendrimer, e.g. PEG, PPG, PEO or polyglycerol
- A61K 47/61: the organic macromolecular compound being a polysaccharide or a derivative thereof
- A61P 7/02: Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
- A61P 9/10: for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
- C07K 14/76: Albumins
- C07K 14/79: Transferrins, e.g. lactoferrins, ovotransferrins
- C07K 2319/30: Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
- C07K 2319/31: fusions, other than Fc, for prolonged plasma life, e.g. albumin
- 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)
- 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)
- A61P: SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS

## Abstract

A soluble polypeptide comprising a modified glycoprotein V (GPV) lacking a functional transmembrane domain for use in the treatment or prevention of a thrombotic disease in a subject, said treatment or prevention comprising administering to the subject an effective amount of said soluble polypeptide.

## Claims

### Claim 1

A method for the treatment and/or prevention of a thrombotic disease in a subject, comprising administering to the subject an effective amount of a soluble polypeptide comprising a modified glycoprotein V (GPV) lacking a functional transmembrane domain,
wherein the modified GPV comprises an amino acid sequence at least 75% identical to amino acids 1-503 of SEQ ID NO:3 or amino acids 1-502 of SEQ ID NO:7, and
wherein the thrombotic disease is selected from the group consisting of thrombo-inflammatory conditions, venous thrombosis, arterial thrombosis, capillary thrombosis, portal vein thrombosis, renal vein thrombosis, jugular vein thrombosis, cerebral venous sinus thrombosis, thrombus formation during or after contacting blood with an artificial surface, atherosclerosis, arthritis, coagulopathy, deep venous thrombosis (DVT), disseminated intravascular coagulopathy (DIC), a chronic or acute thromboembolism, pulmonary thromboembolism, Budd-Chiari syndrome, Paget-Schroetter diseases, stroke, and myocardial infarction.

### Claim 2 (depends on 1)

The method according to claim 1, wherein the modified GPV is a truncated GPV.

### Claim 3 (depends on 1)

The method according to claim 1, wherein the modified GPV consists of a fragment of the extracellular domain of a native GPV.

### Claim 4 (depends on 3)

The method according to claim 3, wherein the native GPV consists of the amino acid sequence of SEQ ID NO:3.

### Claim 5 (depends on 1)

The method according to claim 1, wherein the soluble polypeptide is a non-naturally occurring polypeptide.

### Claim 6 (depends on 5)

The method according to claim 5, wherein the soluble peptide further comprises a half-life-extending moiety.

### Claim 7 (depends on 6)

The method according to claim 6, wherein the half-life-extending moiety is conjugated to the modified GPV.

### Claim 8 (depends on 7)

The method according to claim 7, wherein the half-life-extending moiety is selected from the group consisting of hydroxyethyl starch (HES), polyethylene glycol (PEG), polysialic acids (PSAs), and albumin binding ligands.

### Claim 9 (depends on 6)

The method according to claim 6, wherein the half-life-extending moiety is a heterologous amino acid sequence fused to the modified GPV, either directly or via a linker.

### Claim 10 (depends on 9)

The method according to claim 9, wherein the heterologous amino acid sequence comprises or consists of a polypeptide selected from the group consisting of albumin and a fragment thereof having a length of at least 100 amino acids, immunoglobulin constant regions and fragments thereof, transferrin and fragments thereof, the C-terminal peptide of human chorionic gonadotropin, solvated random chains with large hydrodynamic volume (XTEN), homo-amino acid repeats (HAP), proline-alanine-serine repeats (PAS), afamin, alpha-fetoprotein, Vitamin D binding protein, polypeptides capable of binding under physiological conditions to albumin or immunoglobulin constant regions, and combinations thereof.

### Claim 11 (depends on 1)

The method according to claim 1, wherein the soluble polypeptide is obtained by recombinant expression in mammalian cells.

### Claim 12 (depends on 1)

The method according to claim 1, further comprising administering to the subject an anti-platelet or an anti-coagulant drug.

### Claim 13 (depends on 1)

The method of claim 1, wherein the thrombotic disease is thrombus formation during or after extracorporeal membrane oxygenation (ECMO).

### Claim 14 (depends on 7)

The method of claim 7, wherein the half-life-extending moiety is a fatty acid chain.

### Claim 15 (depends on 9)

The method of claim 9, wherein the heterologous amino acid sequence comprises an Fc fragment.

### Claim 16 (depends on 1)

The method of claim 1, wherein the modified GPV comprises amino acids 1-503 of SEQ ID NO:3 or amino acids 1-502 of SEQ ID NO:7.

### Claim 17 (depends on 1)

The method of claim 1, wherein the modified GPV comprises amino acids 1-518 of SEQ ID NO:3 or amino acids 1-519 of SEQ ID NO:7.

### Claim 18 (depends on 1)

The method of claim 1, wherein the modified GPV comprises amino acids 1-516 of SEQ ID NO:3.

### Claim 19 (depends on 1)

The method of claim 1, wherein the modified GPV lacks the transmembrane domain of a native GPV.