Neko Pharma’s KazanbodyTM core technology was developed from a small thermophilic bacterial protein, making use of naturally existing extreme stability for solving the biophysical and protein engineering problems encountered with human or llama derived binding domains.
We eliminated T-cell receptor epitopes by introducing point mutations to produce a base scaffold molecule with low immunogenicity. CD4+ T cell proliferation time course assays performed on 50 PBMC donors with globally diverse HLA allotypes generated only 2 responses (4%), similar to Herceptin® (6%).
We generated an unparalleled flexible binding surface consisting of three solvent exposed randomized loops grafted onto the surface of the deimmunized scaffold. This binding surface was engineered to exhibit greater flexibility than the induced-fit target binding of human antibody CDRs. This enables a unique recognition of difficult to target epitopes such as peptides, clefts and cavities, providing more diverse drug candidates. The extreme stability of our scaffold enables customized binding surface design on request.
Our scaffold contains no cysteines or disulphide bonds, enabling reliable and cheap E. coli production. Artificial cysteine incorporation enables user controlled conjugation of the number and position of drugs and other molecules.
The extreme stability of our scaffold library (Tm 80℃ – 90℃ for binding clones) is designed to provide you with a reliable engineering solution for exploring a variety of targeting applications, such as bispecific CAR-T, bispecific drug conjugates, bioPROTACs, bispecific T-cell recruitment, and a variety of other multispecific modalities.