IP Library › Granted Patent US 12,139,529
Granted Patent B2
US 12,139,529 · App. 18/298,953 · Granted Nov 12, 2024

Antibody-peptide fusion proteins for treating amyloid disorders

Inventors: Jonathan S. Wall (Knoxville, TN); James S. Foster (Knoxville, TN); Spencer Guthrie (San Francisco, CA); Jaume Pons (San Francisco, CA); Michael L. Klein (San Francisco, CA)
Assignees: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION; ATTRALUS, INC.
C07K16/18A61K51/1093C07K14/001C07K2317/77C07K2317/92C07K2319/30
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Quick Facts
Patent No.
US 12,139,529
App. No.
18/298,953
Granted
Nov 12, 2024
Kind
B2
Abstract

Provided herein are antibody-peptide fusion proteins comprising an amyloid-reactive peptide linked to an antibody. Also provided herein are methods of treating amyloid-based diseases by administering an antibody-peptide fusion protein.

Claims (16)

1. An antibody-peptide fusion protein, comprising:

an antibody that binds to human amyloid fibrils comprising i) a heavy chain and ii) a light chain with an amyloid-reactive peptide fused to the C-terminus of the light chain via a linker,

wherein the heavy chain comprises the amino acid sequence of SEQ ID NO:91, and the light chain with the amyloid-reactive peptide fused to the C-terminus of the light chain via the linker comprises the amino acid sequence of SEQ ID NO:89.

2. A pharmaceutical composition comprising

the antibody-peptide fusion protein of claim 1 and a pharmaceutical acceptable carrier.

3. A polynucleotide encoding an antibody-peptide fusion protein comprising:

an antibody that binds to human amyloid fibrils comprising i) a heavy chain and ii) a light chain with an amyloid-reactive peptide fused to the C-terminus of the light chain via a linker,

wherein the heavy chain comprises the amino acid sequence of SEQ ID NO:91, and the light chain with the amyloid-reactive peptide fused to the C-terminus of the light chain via the linker comprises the amino acid sequence of SEQ ID NO:89.

4. A vector comprising the polynucleotide of claim 3 .

5. A host cell comprising the vector of claim 4 .

6. An antibody-peptide fusion protein that binds to human amyloid fibrils produced by a method comprising:

a) culturing a host cell comprising a vector encoding the antibody-peptide fusion protein under perfusion cell culture conditions suitable for expression of the antibody-peptide fusion protein, wherein the antibody-peptide fusion protein comprises an antibody that binds to human amyloid fibrils comprising i) a heavy chain and ii) a light chain with an amyloid-reactive peptide fused to the C-terminus of the light chain via a linker, wherein the heavy chain comprises the amino acid sequence of SEQ ID NO:91, and the light chain with the amyloid-reactive peptide fused to the C-terminus of the light chain via a linker comprises the amino acid sequence of SEQ ID NO: 89; and

b) recovering the antibody-peptide fusion protein produced by the host cell.

7. The antibody-peptide fusion protein of claim 6 , wherein the method comprises recovering the antibody-peptide fusion protein about every 12-36 hours.

8. The antibody-peptide fusion protein of claim 6 , wherein the host cell is a Chinese hamster ovary (CHO) cell.

9. An antibody-peptide fusion protein that bind to human amyloid fibrils, wherein the fusion protein comprises a first polypeptide, a second polypeptide, a third polypeptide, and a fourth polypeptide, wherein the first polypeptide and the second polypeptide each comprise the amino acid sequence set forth in SEQ ID NO:89, and the third polypeptide and the fourth polypeptide each comprise the amino acid sequence set forth in SEQ ID NO:91.

Assignments (2)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 28, 2023
From: GUTHRIE, SPENCER; PONS, JAUME; KLEIN, MICHAEL L.
To: ATTRALUS, INC.
Reel/Frame 065068/0144 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded May 26, 2023
From: WALL, JONATHAN S.; FOSTER, JAMES S.
To: UNIVERSITY OF TENNESSEE RESEARCH FOUNDATION
Reel/Frame 063779/0234 →
Continuity (3)
Continuation PCTUS2022072413 · May 18, 2022
Provisional Application 63190191 · May 18, 2021
Related Publication 20230416347A1 · Dec 28, 2023
Cited By (1)
US 12,264,195