Overview The concept of antibody allostery describes long-range intramolecular communication between the variable (V) and constant (C) regions.While a growing body of structural, computational, and functional studies challenges the classical model of strict domain independence,
Monoclonal antibodies have become one of the most established modalities in modern drug development, with expanding pipelines across oncology, immunology, and infectious disease. At the same time, the scale and speed of antibody discovery have changed dramatically. New discovery platforms, automatio
Fully human antibodies are monoclonal antibodies whose variable and constant regions are derived entirely from human immunoglobulin sequences. Unlike earlier therapeutic antibodies generated in murine systems and subsequently engineered through chimerization or humanization, fully human antibodies a
Introduction: Persistent Dominance of E. coli as a Protein Expression Platform Escherichia coli remains the most widely used host organism for recombinant protein production due to its rapid growth, inexpensive cultivation, and well-established genetic tools. Despite decades of use, t
Antibody therapeutics have a structural limitation: many targets such as immune checkpoints, costimulatory receptors, and broadly expressed tumor-associated antigens, cannot be engaged at pharmacologically optimal exposures without triggering dose-limiting on-target, off-tumor toxicities. In response, multiple groups are exploring antibody formats, like introducing conditionality.
Recent work in antibody-cytokine fusion proteins reflects a clear engineering objective: retain the immunostimulatory capacity of cytokines while reducing systemic toxicities associated with non-restricted receptor engagement.
Radioligand therapy (RLT), also known as radiopharmaceutical therapy, is quickly becoming a major player in the oncology therapeutics space, specifically radioantibodies.
Biointron’s 2026 Antibody Industry Outlook aims to explore the events and trends of the biopharmaceutical industry for 2026. Last year, 21 novel monoclonal antibody drugs have been approved by China, United States, Europe, and Australia.
Fusion proteins are engineered molecules combining domains from two or more distinct proteins into a single polypeptide chain to endow new or enhanced biological functions. In antibody research and drug development, fusion proteins often incorporate an immunoglobulin framework with targeting, signaling, or effector domains such as cytokines, enzymes, or synthetic peptides.
Antibody-drug conjugates (ADCs) rely critically on the chemical linker as the molecular bridge between the antibody and the cytotoxic payload. This component governs not only stability and pharmacokinetics but also the specificity and mechanism of payload release. Recent research describes computational and chemically innovative strategies to expand the functional and pharmacological space of linkers.
Despite comprising the largest family of druggable membrane proteins, only three G protein-coupled receptor (GPCR)-targeting antibodies have been approved. The human genome has more than 800 GPCRs, which regulate various critical physiological processes, but many GPCRs are expressed poorly, or have unknown ligands and unclear signaling pathways.
In 2025, 21 novel monoclonal antibody (mAb) drugs were approved for the first time worldwide. These approvals represent an expansion of both antibody modality and therapeutic focus, with developments in bispecifics, ADCs, long-acting formulations, and first-in-class mechanisms.