Biointron’s Q2 2026 Antibody Industry Trends report aims to explore the events and trends of the biopharmaceutical industry in April, May, and June. This quarter, six novel monoclonal antibody drugs have received first approval.
TED is a rare, debilitating disease that can cause eye dryness and redness, eyelid swelling or retraction, bulging eyes (proptosis), double vision, and, in severe cases, vision impairment.
Artificial intelligence is changing how researchers think about antibody discovery. For decades, antibody programs have usually started with experimental screening.
Seasonal influenza causes an estimated one billion infections, 3-5 million severe cases, and 300,000-500,000 deaths globally each year. According to a recent review, existing vaccines provide variable protection because their effectiveness depends on how closely vaccine strains match circulating viruses. Influenza also evolves through antigenic drift and, less frequently, antigenic shift, while resistance can reduce the effectiveness of antiviral drugs.
Artificial intelligence can now help researchers analyze antibody sequences, predict structures, prioritize mutations, optimize candidate properties, and generate entirely new antibody sequences. These capabilities are changing what can be proposed computationally, but every proposed sequence raises the practical question: will the antibody actually work?
Degrader-antibody conjugates, or DACs, combine the targeting ability of antibodies with the intracellular activity of targeted protein degraders. Instead of delivering a conventional cytotoxic payload, they are designed to deliver a molecule that eliminates a specific disease-driving protein inside selected cells.
Bispecific antibody-drug conjugates, or BsADCs, combines the payload-delivery function of an ADC with the dual-recognition capacity of a bispecific antibody. Instead of binding one antigen or one epitope, the antibody component can be designed to recognize two different antigens, or two distinct epitopes on the same antigen. This added specificity may improve tumor selectivity, increase internalization, or broaden activity across heterogeneous tumors.
Programmable antibodies can describe several related approaches that make antibody-based systems more designable and controllable. A traditional antibody has two main functional parts: the Fab region, which recognizes a target antigen, and the Fc region, which interacts with immune receptors and helps determine downstream immune activity.
Chemical conjugation is the process of using defined chemical reactions to attach a “payload” to an antibody. That payload can be a cytotoxic drug, imaging agent, radionuclide chelator, oligonucleotide, peptide, protein, or even another antibody fragment. In antibody therapeutics, this matters bec
Antibody drugs, particularly monoclonal antibodies (IgGs), have transformed modern medicine, especially in areas like cancer and autoimmune disease. Now, however, VHH antibodies, also known as nanobodies are increasingly being recognized for their potential in biopharmaceutical applications due to their unique properties such as specificity, small molecule size, high affinity, good stability, flexible delivery routes, and fast tissue penetration.
Monoclonal antibodies (mAbs) have applications across oncology, autoimmune disease, infectious disease, and diagnostics. Historically, antibody development focused on binding specificity, which is the ability to recognize a defined antigen. Now, we have multidimensional characterization, where evaluation of structure, biological activity, immunogenicity, and functional outcomes is integrated.
A global resurgence of measles has been driven by declining vaccination coverage and gaps in herd immunity, renewing interest in antibody-based therapeutic strategies targeting measles virus (MeV). Recent studies demonstrate rapid advances in the identification, structural characterization, and functional evaluation of monoclonal antibodies (mAbs) directed against key viral glycoproteins.