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According to published analyses, approximately 90% of drug candidates fail during clinical development, and this figure may exceed 99% when preclinical stages are included. Learn about antibody developability.

Antibody developability refers to the set of biochemical, biophysical, and structural attributes that influence the manufacturability, stability, and clinical viability of an antibody candidate. Simply, developability assesses the likelihood that a candidate will become a safe and efficacious drug. While biological activity and binding affinity remain central to therapeutic antibody selection, developability has emerged as a critical parameter in determining whether a candidate can advance successfully through preclinical development and into the clinic.

The Festival of Biologics 2025 was held in Basel, Switzerland, from September 30 to October 2, 2025. The event highlighted advances across discovery, development, clinical trials, manufacturing, market access, and fill & finish. As Europe’s largest biologics event,3000+ attendees and 350

The 23rd Annual Discovery on Target conference was held in Boston, MA, USA, from September 22-25, 2025. The event highlighted advances across protein degradation, induced proximity, synthetic biology, AI-enabled design, immune modulation, and 3D organoid modeling, alongside GLP-1 biology, MASH and obesity, ADCs, and multispecifics.

Discover key takeaways from Biointron’s Lunch & Learn with KACTUS at CIC Cambridge, featuring expert talks and lively audience discussions.

The 16th Annual World Bispecific Summit was held in Boston, MA, USA, from September 9-11. The event theme was: “Enhance VEGFxPD1 Mechanistic Understanding, Target Selectivity & Binding Affinity to Supercharge the Discovery & Development of Bispecifics in Oncology & Autoimmune Diseases”

Recombinant protein technology emerged from a series of foundational discoveries in molecular biology during the mid-20th century. These began with the identification of DNA as the carrier of genetic information in the 1940s, followed by the one gene–one enzyme hypothesis by Beadle and Tatum, and culminated in Watson and Crick's 1953 model of DNA structure, aided by X-ray diffraction data from Rosalind Franklin.

Recombinant antibody (rAb) production in mammalian cells is a critical technology for biologics development. Mammalian systems are preferred for their ability to perform human-like post-translational modifications (PTMs), particularly glycosylation, as well as their capacity for proper folding and assembly of complex, disulfide-rich proteins such as immunoglobulins.

Hybridoma technology, developed by Köhler and Milstein in 1975, introduced a method for the generation of monoclonal antibodies (mAbs) through the fusion of antigen-specific B lymphocytes with immortal myeloma cells. This approach enabled the long-term culture of hybrid cells—termed hybridomas—that produce highly specific antibodies targeting a single epitope.

Antibody fragments have become indispensable in modern biotechnology due to their smaller size, improved tissue penetration, and suitability for engineered constructs. Among these, camelid VHH nanobodies (single-domain antibodies) and single-chain variable fragments (scFvs) represent two widely studied and applied formats. Both can be produced recombinantly and tailored for diagnostic or therapeutic use, yet their origins, molecular structures, and functional properties are distinct.

Single-domain antibodies (sdAbs), often referred to as VHHs or nanobodies, are derived from the heavy-chain-only antibodies found in camelids such as llamas and alpacas. They are the smallest naturally occurring antibody fragments, about 15 kDa in size, and consist of a single variable domain.

VHH antibodies, also called single-domain antibodies or nanobodies, are the smallest functional fragments of antibodies capable of binding antigens. They originate from the heavy-chain-only antibodies found in camelids such as llamas and camels. Unlike conventional antibodies, which require both heavy and light chains for antigen recognition, VHHs operate as a single domain.