# US 11,440,942 B2 · Complement factor based affinity chromatography > Agents: this data is available as JSON from the patentgrep API and MCP server — see https://patentgrep.com/llms.txt - Number: US 11,440,942 B2 - Document ID: US11440942B2 - Status: Granted - Kind: B2 - Application number: 16/354,627 - Filed: 2019-03-15 - Published: 2020-01-02 - Granted: 2022-09-13 - Earliest claimed: 2016-09-19 - Assignees: Hoffmann-La Roche Inc. - Applicants: Hoffmann-La Roche Inc. - Inventors: Alexander Knaupp; Laurent Lariviere; Petra Rueger; Tilman Schlothauer; Stefan Seeber - Web page: https://patentgrep.com/patent/US11440942B2 ## CPC - C07K 14/472: {Complement proteins, e.g. anaphylatoxin, C3a, C5a} - B01D 15/3804: {Affinity chromatography} - B01D 15/3809: {of the antigen-antibody type, e.g. protein A, G or L chromatography} - C07K 1/22: Affinity chromatography or related techniques based upon selective absorption processes - C07K 16/18: against material from animals or humans - C07K 2317/92: Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value - C07K 2317/94: Stability, e.g. half-life, pH, temperature or enzyme-resistance - C07K 2319/00: Fusion polypeptide - G01N 2333/4716: Complement proteins, e.g. anaphylatoxin, C3a, C5a - 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) - B01D: SEPARATION (separating solids from solids by wet methods B03B, B03D; by pneumatic jigs or tables B03B; by other dry methods B07; magnetic or electrostatic separation of solid materials from solid materials or fluids, separation by high-voltage electric fields B03C; centrifuges, vortex apparatus B04; presses per se for squeezing-out liquid from liquid-containing material B30B9/02; treatment of water C02F, e.g. softening by ion-exchange C02F1/42; {arrangements of air intake cleaners in gas turbine plants F02C7/05} ; arrangements or mounting of filters in air-conditioning, air-humidification or ventilation F24F13/28) - G01N: INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES (measuring or testing apparatus or processes other than immunoassay, involving enzymes or microorganisms C12M, C12Q) ## Abstract Herein is reported a fusion polypeptide according to formula I (TAG-X1-C1qA-X2-C1qB-X3-C1qC-X4), comprising a fragment of SEQ ID NO: 01 (C1qA), a fragment of SEQ ID NO: 03 (C1qB), a fragment of SEQ ID NO: 05 (C1qC) and optionally a tag (TAG). ## Claims ### Claim 1 A fusion polypeptide according to formula I TAG-X1-C1qA-X2-C1qB-X3-C1qC-X4 (formula I) wherein X1 denotes a first peptidic linker, X2 denotes a second peptidic linker, X3 denotes a third peptidic linker, X4 denotes a fourth peptidic linker, X1, X2, X3, X4 are independently of each other either present or absent, TAG is an amino acid sequence tag, TAG can be present or absent, C1qA has the amino acid sequence of SEQ ID NO: 07 is a fragment of SEQ ID NO: 01, C1qB has the amino acid sequence of SEQ ID NO: 08 is a fragment of SEQ ID NO: 03, C1qC has the amino acid sequence of SEQ ID NO: 09 is a fragment of SEQ ID NO: 05, and - denotes a peptide bond. ### Claim 2 (depends on 1) The fusion polypeptide according to claim 1, wherein X1, X2 and X3 are present and X4 is absent or wherein X2, X3 and X4 are present and X1 is absent. ### Claim 3 (depends on 1) The fusion polypeptide according to claim 1, wherein X1 has the amino acid sequence of SEQ ID NO: 10, X2 has the amino acid sequence of SEQ ID NO: 11 or 12, and X3 has the amino acid sequence of SEQ ID NO: 13 or 14, or wherein X2 has the amino acid sequence of SEQ ID NO: 13 or 14, X3 has the amino acid sequence of SEQ ID NO: 11 or 12 and X4 has the amino acid sequence of SEQ ID NO: 10. ### Claim 4 (depends on 1) The fusion polypeptide according to claim 1, wherein TAG is present and has the amino acid sequence of SEQ ID NO: 15. ### Claim 5 (depends on 1) A multimeric non-covalent complex comprising 2 to 6 fusion polypeptides according to claim 1. ### Claim 6 (depends on 5) The multimeric non-covalent complex according to claim 5, wherein in at least one of the fusion polypeptides TAG is present and in at least one of the fusion polypeptides TAG is absent. ### Claim 7 (depends on 1) An affinity chromatography ligand comprising the fusion polypeptide according to claim 1. ### Claim 8 (depends on 7) The affinity chromatography ligand according to claim 7, wherein the fusion polypeptide or the complex is immobilized on a solid phase. ### Claim 9 (depends on 8) The affinity chromatography ligand according to claim 8, wherein the solid phase is a chromatography material. ### Claim 10 (depends on 5) An affinity chromatography ligand comprising the multimeric non-covalent complex according to claim 5. ### Claim 11 (depends on 10) The affinity chromatography ligand according to claim 10, wherein the complex is immobilized on a solid phase. ### Claim 12 (depends on 11) The affinity chromatography ligand according to claim 11, wherein the solid phase is a chromatography material.