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Recently, isolated immunoglobulin constant CH2 domains were proposed as scaffolds for construction of libraries containing diverse binders that could confer some effector functions. As a fragment in all IgGs, which are at high concentrations in blood, CH2-based therapeutics are likely to be well tolerated in therapeutic concentrations. CH2 binders can also be engineered to be selective so as to retain some of the effector functions that are possessed only by IgGs and not by other scaffolds.
NCI scientists discovered a novel fully human antibody (anti-CH2 Fab m01m1) that could be used safely in vitro and in vivo for the detection of CH2 and related targets, such as Fc and IgG. More specifically, anti-CH2 Fab m01m1 recognizes a conformational epitope on CH2 so it can be used to monitor conformational changes in CH2 and to select the proper folded isolated CH2 domains. Anti-CH2 Fab m01m1 is a powerful research reagent for developing CH2-based novel therapeutics (nanoantibodies, nAbs).
Discovery (Lead Identification)
P. Prabakaran et al. Structure of an isolated unglycosylated antibody C(H)2 domain.
D.S. Dimitrov, Engineered CH2 domains (nanoantibodies).
R. Gong et al. Engineered human antibody constant domains with increased stability.
X. Xiao et al. A large library based on a novel (CH2) scaffold: identification of HIV-1 inhibitors.
G. Wozniak-Knopp et al. Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds.
Original Article: Human Antibody for Deploying CH2-Based TherapeuticsNEXT ARTICLE
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An antibody is a protein produced by the body's immune system when it detects harmful substances, called antigens. Examples of antigens include microorganisms (such as bacteria, fungi, parasites, and viruses) and chemicals. Antibodies may be produc...