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US 11,535,668 B2Granted
Inducible monovalent antigen binding protein
AssigneeHarpoon Therapeutics, Inc.
InventorsPatrick Baeuerle, Holger Wesche
Life of this patent
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Abstract
Disclosed herein are inducible monovalent target-binding proteins which are activated upon protease cleavage. Pharmaceutical compositions comprising the binding proteins disclosed herein and methods of using such formulations are further provided.
Claims20
An inducible monovalent target-binding protein, wherein the protein comprises a first polypeptide chain and a second polypeptide chain,
- the first polypeptide chain comprising:
- a VH target-binding domain (VH), an inactive VL domain (iVL) that binds to the VH domain, a linker (L1), and a first monomeric Fc domain (Fcl) comprising a CH3 and a CH2 domain;
- the second polypeptide chain comprising:
- a VL target-binding domain (VL), an inactive VH domain (iVH) that binds to the VL domain, a linker (L6), a second monomeric Fc domain (Fc2) comprising a CH3 and a CH2 domain;
- wherein the iVL and the iVH each comprise at least one protease cleavage site, wherein upon activation by protease cleavage of the at least one protease cleavage site of both the iVL and the iVH, the VH and the VL associate to form an active target-binding domain, and wherein the CH3 domains of the Fcl and Fc2 form a heterodimer.
2 more elements
An inducible monovalent target-binding protein, wherein the protein comprises a first polypeptide chain and a second polypeptide chain,
- the first polypeptide chain comprising:
- a VH target-binding domain (VH), an inactive VL domain (iVL) that binds to the VH domain, a linker (L1), and a first monomeric Fc domain (Fcl) comprising a CH3 and a CH2 domain;
- the second polypeptide chain comprising:
- a VL target-binding domain (VL), an inactive VH domain (iVH) that binds to the VL domain, a linker (L6), a second monomeric Fc domain (Fc2) comprising a CH3 and a CH2 domain;
- wherein the L1 and L6 each comprise at least one protease cleavage site, wherein upon activation by protease cleavage of the at least one protease cleavage site of both L1 and L6, the VH and the VL associate to form an active target-binding domain, and wherein the CH3 domains of the Fcl and Fc2 form a heterodimer.
2 more elements
Dependencies are inferred from the claim text.