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AssigneesBoard of Regents, The University of Texas System, Medlmmune, LLC
InventorsWILLIAM DALL'ACQUA, LESLIE S. JOHNSON, ELIZABETH SALLY WARD OBER
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The present invention provides molecules, including IgGs, non-IgG immunoglobulins, proteins and non-protein agents, that have increased in vivo half-lives due to the presence of an IgG constant domain, or a portion thereof that binds the FcRn, having one or more amino acid modifications that increase the affinity of the constant domain or fragment for FcRn. Such proteins and molecules with increased half-lives have the advantage that smaller amounts and or less frequent dosing is required in the therapeutic, prophylactic or diagnostic use of such molecules.
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A modified human or humanized IgG comprising a human IgG constant domain comprising one or more amino acid modifications relative to a wild-type human IgG constant domain, wherein the modified human or humanized IgG has an increased half-life compared to the half-life of a human or humanized IgG having the wild-type human IgG constant domain, and wherein the one or more amino acid modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436.
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A fusion protein comprising a non-IgG polypeptide covalently linked to a modified human IgG constant domain, or a fragment thereof that binds to FcRn, said modified human IgG constant domain or fragment comprising one or more amino acid modifications relative to a wild-type human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, and wherein said fusion protein has a longer half life than the non-IgG polypeptide alone.
The fusion protein according to claim 21, 22, or 23, wherein at least one of the amino acid modifications is an amino acid substitution.
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A molecule, comprising a non-protein agent conjugated to a modified human IgG constant domain, or a fragment thereof that binds to FcRn, said modified human IgG constant domain or fragment comprising one or more amino acid modifications relative to a wild-type human IgG constant domain, wherein the one or more modifications are at one or more of positions 251-256, 285-290, 308-314, 385-389, and 428-436, and wherein said molecule has a longer half life than the non-protein agent alone.
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Dependencies are inferred from the claim text.