Gregory Winter

Sir Gregory Winter shared the 2018 Nobel Prize in Chemistry with Frances Arnold and George Smith for his work applying phage display technology to the engineering of therapeutic antibodies. Winter adapted George Smith's phage display method—originally used for peptide display—to create libraries of antibody fragments on the surface of bacteriophages.

Phage display is a technique in which foreign proteins are genetically fused to a coat protein of a bacteriophage so that they are displayed on the virus's surface. Winter used this approach to create large libraries of antibody variable regions displayed on phage particles, which could then be selected through repeated rounds of binding to a target antigen to evolve antibodies with high affinity and specificity.

Winter's phage display technology was central to the development of adalimumab (Humira), the first fully human monoclonal antibody approved by the FDA (in 2002) as a therapeutic drug. Adalimumab targets tumor necrosis factor alpha (TNF-α) and has been used to treat rheumatoid arthritis, Crohn's disease, psoriasis, and other autoimmune conditions.

Winter carried out his phage display and antibody engineering research at the Medical Research Council (MRC) Laboratory of Molecular Biology in Cambridge, England. He also co-founded Cambridge Antibody Technology (CAT), a biotechnology company that commercialized phage display-derived antibody therapeutics.