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Efforts to engineer antibody-based therapeutics, to date, have encountered technical limitations due to the relatively large fragment size and short fragment half-life. Antibody fragments are emerging as promising biopharmaceuticals because of their relatively small size and other unique properties. However, compared with full-size antibodies, these antibody fragments lack the ability to bind to some Fc receptor and have reduced half-lives.
NCI scientists have developed small (∼27 kDa) antibody fragments that are potentially useful for therapeutic development. These are monomeric IgG fragment (mFc) compositions; they have long half-lives, are functional (pH dependent binders of neonatal Fc receptor - FcRn); soluble, and they express in E. coli efficiently. The molecules may serve as a platform for development of engineered mFc-based antibodies and fusion proteins with therapeutic applications: the smaller size may allow for superior access to targets and tissues compared to full sized mAbs and larger fragment-based therapeutics, while also retaining important functional characteristics. The IgG Fc is a dimer of two constant domains (CH2-CH3 chains). The Fc has a long half-life, which makes it promising as a candidate for engineering antibody therapeutics.
Therapeutics - human and veterinary, engineered antibody and fusion proteins.
Discovery (Lead Identification)
Ying T, et al. Soluble monomeric IgG1 Fc.
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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...
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