Available Technology

Small, Stable, Functional, Soluble, Monomeric IgG1 Fc Molecules Engineered Therapies

This technology relates to small (~27 kDa) antibody fragments that are potentially useful for therapeutic development. These are monomeric IgG fragment crystalizable (mFc) compositions; they are long half-lived, functional (pH dependent binders of neonatal Fc receptor - FcRn); and they are soluble and express efficiently inE. coli. These molecules may serve as a platform for development of engineered mFc-based antibodies and fusion proteins with therapeutic applications. Efforts to engineer antibody-based therapeutics, to date, have encountered technical limitations due to the relatively large fragment size and short fragment half-life. The IgG fragment crystalizable (Fc) is a dimer of two constant domains (CH2-CH3 chains). Fc has a long half-life, which makes it promising as a candidate for engineering antibody therapeutics. Fusion proteins based on Fc dimer molecules demonstrate extended half-life, due to the ability to bind FcRn at acidic pH. However, the relatively large size of the Fc domains (~50 kD) is not optimal. This technology uses smaller (~27 kDa) mFc compositions that retain efficient binding to human FcRn and demonstrate long half-life. These mFc compositions are promising for the development of novel therapeutics because 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 function characteristics.

Patent Abstract: 

This technology relates to small (~27 kDa) antibody fragments that are potentially useful for therapeutic development. These are monomeric IgG fragment crystalizable (mFc) compositions; they are long half-lived, functional (pH dependent binders of neonatal Fc receptor - FcRn); and they are soluble and express efficiently inE. coli. These molecules may serve as a platform for development of engineered mFc-based antibodies and fusion proteins with therapeutic applications. Efforts to engineer antibody-based therapeutics, to date, have encountered technical limitations due to the relatively large fragment size and short fragment half-life. The IgG fragment crystalizable (Fc) is a dimer of two constant domains (CH2-CH3 chains). Fc has a long half-life, which makes it promising as a candidate for engineering antibody therapeutics. Fusion proteins based on Fc dimer molecules demonstrate extended half-life, due to the ability to bind FcRn at acidic pH. However, the relatively large size of the Fc domains (~50 kD) is not optimal. This technology uses smaller (~27 kDa) mFc compositions that retain efficient binding to human FcRn and demonstrate long half-life. These mFc compositions are promising for the development of novel therapeutics because 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 function characteristics.

Benefits 
Smaller size results better tissue penetration, reduced steric hindrance, increased therapeutic efficiency and lower cost.
Inventors: 

Dimiter Dimitrov

Patent Number: 
61612,138 PCT Application No. PCTUS1331593 US A
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