AffiRocks are an immensely stable protein scaffold

The AffiRock protein scaffold is derived from a bacteria that grows in hydrothermal vents at up to 90°C (that is almost 200°F),  affording rock-hard stability and providing an ideal platform for protein engineering.   


AffiRocks offer unique binding site diversity

The AffiRock protein scaffold leverages binding sites with three very different tertiary structures all on one small, stable protein.  This provides paratope diversity at a level beyond only randomization of surface amino acids.  Phage display library screening and subsequent affinity maturation engineering will enable the development of high affinity constructs specifically recognizing almost any protein target.


AffiRocks are small and modular

The AffiRock protein scaffold is extremely small which enables:

        • leveraging renal clearance for molecular imaging applications
        • increased penetration of tissue (or tumors)

…yet modular to enable:

        • multimerization for avidity or multi-target specificity
        • fusion-engineering to other biologics
        • site-specific chemical conjugation to drugs, toxins, or detection labels


AffiRocks have a low risk for immunogenicity

The AffiRock protein scaffold is such an unusually small and stable protein that it is at a very low risk for inducing immunogenicity.  Additionally, AffiRock Biologics has a human AffiRock protein scaffold, derived from an almost structurally identical orthologous human protein domain; which further mitigates concerns of immunogenecity.