This guide shows how single-domain antibodies can unlock crypitic epitopes, streamline CAR-T design, and sepped up the path to multispecific biologics.
Why VHH matters today
Camelid single-domain antibodies pack high affinity and exceptional stability into a footprint of about fifteen kilodaltons. They reach grooves that full IgGs cannot, tolerate harsh process conditions, and lend themselves to rapid genetic fusion.
Over the past decade VHH binders have moved from laboratory curiosity to clinical reality, with the first approvals for blood-brain barrier shuttles, neutralising biologics, and imaging agents. Their small coding sequence fits easily into viral or mRNA vectors, which opens the door to in vivo delivery strategies that are hard to realise with larger formats.
Inside this guide
The chapters walk through each stage of a VHH program, starting with immunisation and naive libraries, progressing through phage or yeast display selections, and closing with engineering options such as bispecific linkages and half-life extension tags.
Real experiment timelines and decision trees appear throughout, giving you a realistic picture of checkpoints, material needs, and cost drivers. Short case highlights illustrate how researchers have used VHH domains in immuno-oncology, high-definition imaging, intracellular inhibition, and diagnostic assays.
We build lasting partnerships
Arrange a no-cost consultation at fortislife.com/vhh-discovery or email [email protected]. Our PhD-level team has completed hundreds of antibody projects for partners ranging from academic labs to global biotechs.
