Binding proteins to the constant region of immunoglobulin G

{
  "publication_number": "US9493547B2",
  "country": "US",
  "kind": "B2",
  "title": "Binding proteins to the constant region of immunoglobulin G",
  "abstract": "The present invention provides polypeptides that bind to immunoglobulin G and methods for their use.",
  "claims": [
    "1. A polypeptide comprising the amino acid sequence of general formula 1 Z1-Z2-Z3 (SEQ ID NO: 1), wherein Z1 is EY(A/C)VSxTADxxxH (SEQ ID NO: 184); Z2 is GxxxxLxRxAVKGxKP (SEQ ID NO: 185); and Z3 is a xxxQQxxFYMxxx (SEQ ID NO: 186), wherein x is any amino acid.",
    "2. The polypeptide of claim 1, wherein Z1 is selected from the group consisting of (SEQ ID NO: 15) EYCVSRTAVDAKKH; (SEQ ID NO: 16) EYAVSRTAVDALKH; (SEQ ID NO: 17) EYCVSRTAVDALKH; (SEQ ID NO: 18) EY(A/C)VSRTA(E/V/L/M/A/I/T)DALKH; (SEQ ID NO: 19) EY(A/C)VSRTA(E/V/L/R/M/A)DALKH; (SEQ ID NO: 20) EY(A/C)VSRTA(E/V/M/A/I/T)DALKH; (SEQ ID NO: 21) EY(A/C)VSRTAVDALKH; (SEQ ID NO: 22) EY(A/C)VSRTA(V/M)DALKH; (SEQ ID NO: 23) EY(A/C)VSRTAMDALKH; (SEQ ID NO: 24) EY(A/C)VSRTAADALKH; (SEQ ID NO: 25) EY(A/C)VSRTAMDALKH; (SEQ ID NO: 26) EY(A/C)VSRTALDALKH; (SEQ ID NO: 27) EY(A/C)VSRTAIDALKH; (SEQ ID NO: 28) EY(A/C)VSRTATDALKH; (SEQ ID NO: 29) EY(A/C)VSRTAVDALKH (SEQ ID NO: 30) EYAVSRTAMDALKH; (SEQ ID NO: 31) EYAVSRTAADALKH; (SEQ ID NO: 32) EYAVSRTAMDALKH; (SEQ ID NO: 33) EYAVSRTALDALKH; (SEQ ID NO: 34) EYAVSRTAIDALKH; (SEQ ID NO: 35) EYAVSRTATDALKH; (SEQ ID NO: 36) EYCVSRTAMDALKH; (SEQ ID NO: 37) EYCVSRTAADALKH; (SEQ ID NO: 38) EYCVSRTAMDALKH; (SEQ ID NO: 39) EYCVSRTALDALKH; (SEQ ID NO: 40) EYCVSRTAIDALKH; and (SEQ ID NO: 41) EYCVSRTATDALKH.",
    "3. The polypeptide of claim 1, wherein Z3 is selected from the group consisting of: (SEQ ID NO: 47) EMEQQAFFYMKLR; (SEQ ID NO: 48) EMEQQALFYMKLR; (SEQ ID NO: 49) TFEQQSFFYMSLK; (SEQ ID NO: 51) (B5)(B6)EQQ(S/A)(F/L)FYM(B5)L(K/R), where B5 and B6 are independently any amino acid; (SEQ ID NO: 52) (G/R/S/M/P/W/V/T/R)(M/L/I/A/E/F)EQQ(S/A) (F/L)FYM(B5)L(K/R); (SEQ ID NO: 53) (V/H/K/W)(M/W/I/L/H)EQQ(S/A)(F/L)FYM(B5)L(K/R); (SEQ ID NO: 54) EMEQQALFYMKLK; (SEQ ID NO: 55) VWEQQSFFYMVLK; (SEQ ID NO: 56) HWEQQSFFYMLLK; (SEQ ID NO: 57) HMEQQSFFYMMLK; (SEQ ID NO: 58) KIEQQSFFYMMLK; (SEQ ID NO: 59) WLEQQSFFYMALK; (SEQ ID NO: 60) WLEQQSFFYMQLK; (SEQ ID NO: 61) WLEQQAFFYMELK; (SEQ ID NO: 62) WLEQQSFFYMKLK; (SEQ ID NO: 63) FLEQQSFFYMRLK; (SEQ ID NO: 64) WHEQQSFFYMMLK; (SEQ ID NO: 65) WHEQQSFFYMRLK; (SEQ ID NO: 66) EMEQQALFYMKLK; (SEQ ID NO: 67) GMEQQSFFYMILK; (SEQ ID NO: 68) RLEQQSFFYMTLK; (SEQ ID NO: 69) SLEQQSFFYMNLK; (SEQ ID NO: 70) MIEQQSFFYMRLK; (SEQ ID NO: 71) PIEQQSFFYMHLK; (SEQ ID NO: 72) WLEQQSFFYMHLK; (SEQ ID NO: 73) VLEQQSFFYMDLK; (SEQ ID NO: 74) WAEQQSFFYMGLK; (SEQ ID NO: 75) TEEQQSFFYMTLK; (SEQ ID NO: 76) TFEQQSFFYMSLK; and (SEQ ID NO: 77) RLEQQSFFYMSLK.",
    "4. The polypeptide of claim 1, wherein Z2 has the amino acid sequence (SEQ ID NO: 85) G(F/V)(E/D)(V/G)(Y/C)L(L/F)R(D/E/N)AVKG(I/V/F)KP.",
    "5. The polypeptide of claim 1, wherein the polypeptide comprises one of the following amino acid sequences selected from the group consisting of SEQ ID NOs: 117-119.",
    "6. The polypeptide of claim 1, wherein the polypeptide comprises the amino acid sequence of general formula 5, Z4-Z1-Z2-Z3 (SEQ ID NO: 8), wherein Z4 is a peptide of at least between 100-200 amino acids in length.",
    "7. The polypeptide of claim 6, wherein Z4 comprises the amino acid sequence of SEQ ID NO: 120.",
    "8. The polypeptide of claim 1, wherein the polypeptide comprises one of the following amino acid sequences selected from the group consisting of SEQ ID NOs: 141-169 and 172-182.",
    "9. A pharmaceutical composition comprising the polypeptide of claim 1 and a pharmaceutically acceptable carrier.",
    "10. A composition, comprising the polypeptide of claim 1 =bound to a solid support.",
    "11. The polypeptide of claim 1, wherein the polypeptide comprises the amino acid sequence of SEQ ID NO:143.",
    "12. The polypeptide of claim 2, wherein Z3 is selected from the group consisting of SEQ ID NOs: 47-49 and 51-77.",
    "13. The polypeptide of claim 2, wherein Z2 has the amino acid sequence of SEQ ID NO:85.",
    "14. The polypeptide of claim 12 wherein Z2 has the amino acid sequence of SEQ ID NO:85.",
    "15. The polypeptide of claim 3 wherein Z2 has the amino acid sequence of SEQ ID NO:85.",
    "16. A method for purifying antibodies or Fc fusion proteins, comprising (a) contacting a sample comprising antibodies or Fc fusion proteins with one or more polypeptides according to claim 1 under suitable conditions for binding of antibodies in the sample to the one or more polypeptides to form antibody-polypeptide complexes; and (b) dissociating the antibody from the antibody-polypeptide complexes, to isolate the antibody.",
    "17. A method for detection of an antibody or Fc fusion protein in a sample, comprising (a) contacting a sample comprising antibodies or Fc fusion proteins with one or more polypeptides according to claim 1 under suitable conditions for binding of antibodies or Fc fusion protein in the sample to the one or more polypeptides to form antibody-polypeptide complexes; and (b) detecting the antibody-polypeptide complexes."
  ],
  "description_excerpt": "Recombinant monoclonal antibodies and Fc-fusion proteins have become an important class of biological pharmaceuticals and research reagents. Their manufacture typically involves mammalian cells as the expression host and affinity chromatography as a key purification step. While upstream processes such as cell-line development and engineering have significantly enhanced antibody yields, the downstream purification steps remain expensive and reduce productivity. The vast majority of antibody purification pipelines employ a Protein A-based purification step, which contributes to the majority of the raw-material costs 1, 2. Antibody elution from a Protein A column is typically achieved by lowering the pH to 3. However, at such low pH, aggregation and denaturation of the antibody and of Fc-fusion proteins can easily occur.\n\nIn a first aspect, the present invention provides polypeptides comprising or consisting of an amino acid sequence of general formula 1 Z1-Z2-Z3 (SEQ ID NO: 1), wherein\n\nZ1 is a peptide with an amino acid sequence according to general formula 2: X1-S-X2 (SEQ ID NO: 2), wherein\n\nZ2 is a peptide of between 17 and 50 amino acid residues; and\n\nZ3 is a peptide with an amino acid amino acid sequence according to general formula 3: B1-Q-B2-F-Y-B3 (SEQ ID NO: 3)\n\nIn one embodiment, X2 may be R-X10 (SEQ ID NO: 50), wherein X10 is any 8 amino acids. In another embodiment, X2 may be a peptide of general formula 4: R-J1-V-J2 (SEQ ID NO: 4), wherein\n\nIn one embodiment, X2 may be RTA(X3)D(A/F)(L/R/K)(K/L)H (SEQ ID NO: 5); wherein X3 is any amino acid.",
  "cpc": [
    "C07K 16/00",
    "A61K 38/50",
    "C07K 1/22",
    "C07K 14/001",
    "C12N 9/80",
    "C12Y 305/01019",
    "G01N 33/6854"
  ],
  "ipc": [
    "A61K 38/50",
    "C07K 16/00",
    "C12N 9/80",
    "G01N 33/68",
    "A61K 38/00",
    "A61K 38/16",
    "C07K 1/00",
    "C07K 1/22",
    "C07K 14/00",
    "C07K 17/00",
    "C07K 5/00",
    "C07K 7/00"
  ],
  "assignees": [
    "University of Washington Center for Commercialization"
  ],
  "inventors": [
    "David Baker",
    "Eva-Maria STRAUCH",
    "Sarel Jacob Fleishman"
  ],
  "filing_date": "2013-03-25",
  "publication_date": "2016-11-15",
  "grant_date": "2016-11-15",
  "priority_date": "2012-03-26",
  "application_number": "US-201314387699-A",
  "family_id": "48096249",
  "cited_by_count": 2,
  "citations": [
    "US20030181692A1",
    "US20040214272A1",
    "EP1923464A1"
  ]
}