iBodies technology

Polymer-based antibody mimetics: inhibitors + antibody

iBodies, the novel macromolecules designed to fully substitute antibodies in common biochemical methods, are now ready for routine use in laboratories. iBodies were successfully tested in ELISA, flow cytometry, confocal microscopy, Western Blotting, protein immobilization and immunoprecipitation methods^. These fully synthetic antibody mimetics consist of N-(2-hydroxypropyl) methacrylamide (HPMA) copolymer backbone decorated with low-molecular-weight functional groups: a targeting ligand, an affinity anchor and an imaging probe (Fig.1). In theory, iBodies can be custom designed towards any protein of interest (provided a ligand is known) and tailored based on the intended applications.

 

               Fig.1: Schematic structure of iBody

 

iBodies vs. Antibodies

• + Flexible platform (the type and number of functional groups per iBody molecule is adjustable)
• + High chemical stability
• + Easy preparation and chemical modification
• + Fully synthetic – produced in non-animal based systems
• + Means of protein targeting via an active site provides possibility to target groups of homologous proteins
• + Possibility to target mouse proteins
• + Lower batch to batch variability
• - iBodies can only be designed against targets to which ligands/inhibitors are known

Application

Current stage of development enables the use of iBodies primarily in the scientific research in the above mentioned applications where specific antibodies against proteins  are commonly used (confocal microscopy, flow cytometry, immunoprecipitation, ELISA etc.). The anti-His-tag iBody, representing our most-developed iBody, is an excellent alternative for antibodies used in western blotting (Fig.2).

Fig.2: Detection of 10xHis and 6xHis-tagged proteins on western blot. Comparison of detection with commercially available mAbs.

IP owners & patent status

Institute of Organic Chemistry and Biochemistry, the Czech Academy of Sciences, Prague
Institute of Macromolecular Chemistry, the Czech Academy of Sciences, Prague
Charles University, Prague
Patent applications: PV 2015-19, PV 2015-20, PCT: CZ201605002, CZ201605003

 

References:

1. Angewandte Chemie Int Edit 2016, 55, 2356-2360

1. Nature Methods 2013, 10, 703-707