Years of camelid repertoire analysis inform a computationally optimized synthetic single domain library
Camelids produce single domain antibodies that consist only of a VH domain, providing numerous advantages over traditional IgG antibodies for both reagent and therapeutic purposes. They are smaller in size, easier to manufacture and engineer, and can access epitopes normally sterically hindered to an IgG.
Our Tungsten design incorporates a decade of computational optimization, including variations that are tolerated on the VHH fold. The library includes extensive experimental optimization of two frameworks: an optimal camelid framework for reagent development, and an optimal human VH3-23 framework for therapeutic development. The library has been thermostabilized and purified for functionally folded members and panning campaigns are producing single digit nanomolar binders against multiple targets. Tungsten 1.0 is available in phage display format and can be adapted to any other display platform that our partners have licensed access to, including mammalian display, yeast display, bacterial display and ribosome display.