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DOI:10.1038/s41557-024-01507-y

Multi-Payload Antibody–Drug Conjugates

Antibody–drug conjugates (ADCs) have emerged as a revolutionary class of targeted cancer therapies, combining the specificity of monoclonal antibodies with the potent cytotoxicity of small-molecule drugs. While traditional ADCs typically carry a single type of cytotoxic payload, recent advancements have explored the incorporation of multiple payloads within a single ADC.   Cancer treatment has significantly […]

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Affinity maturation refers to the process of improving antibody affinity and binding interactions to target antigens. This is done naturally in vivo by somatic hypermutation and clonal selection in mammalian B cells, but it can also be done in the lab in vitro by mutagenesis and selection for therapeutic applications. In vivo When a host is repeatedly exposed to the same antigen, the antibodies produced by their immune response will have increasingly greater affinity, avidity, and anti-pathogen activity. This occurs due to somatic hypermutation in the variable CDRs (complementarity-determining regions) of immunoglobulin genes in B cells, and takes place in germinal centers (structures within secondary lymphoid tissues). Clonal selection takes place when follicular dendritic cells of the germinal centers present antigens to the B cells, with only the most competitive B cells surviving to stably conjugate with follicular B helper T cells. After several rounds of selection, high-affinity antibodies will be produced.1 In vitro Similar to the in vivo process, in vitro affinity maturation is used to optimize antibodies, antibody fragments, or other peptides by diversifying the antibody base sequence and isolating higher-affinity binders. FCMES-AM™ (Full Coverage Mammalian Expression System for Affinity Maturation) is Biointron's proprietary platform for affinity maturation. Each amino acid in the CDR region will be mutated to the other 17 amino acids (except Cysteine and Methionine) with equal ratios. The clones will be expressed in a mammalian system, and an ELISA binding assay will be conducted as an initial test. This will be followed by SPR (surface plasmon resonance) or FACS (fluorescence-activated cell sorting) for further affinity measurements.The process is as follows: Site-directed saturated mutation High-throughput mammalian cell expression ELISA and sequencing to identify hot spots Combinatorial mutation design and characterization At Biointron, we are dedicated to accelerating antibody discovery, optimization, and production. Our advantages in affinity maturation include: No-bias Site Saturation Mutagenesis in CDR Regions Guaranteed at least 5-fold Affinity Improvement Our team of experts can provide customized solutions that meet your specific research needs. Contact us to learn more about our services and how we can help accelerate your research and drug development projects. References: Doria-Rose, N. A., & Joyce, M. G. (2015). Strategies to guide the antibody affinity maturation process. Current Opinion in Virology, 11, 137. https://doi.org/10.1016/j.coviro.2015.04.002

Affinity Maturation

Affinity maturation refers to the process of improving antibody affinity and binding interactions to target antigens. This is done naturally in vivo by somatic hypermutation and clonal selection in mammalian B cells, but it can also be done in the lab in vitro by mutagenesis and selection for therapeutic applications.  In vivo  When a host

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DOI: 10.3390/antibiotics10121530

Core Functions of Antibodies

The core functions of antibodies within the immune system are highly diverse and important, serving as the body’s primary defense against a variety of pathogens. These Y-shaped proteins, produced by B cells, are not only tasked with the direct neutralization of pathogens but also play a pivotal role in orchestrating a broader immune response. Through

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What Are Antibody Mimetics?

Antibody mimetics, also known as non-immunoglobulin scaffolds, are engineered proteins designed to mimic the antigen-binding properties of antibodies. Unlike traditional antibodies, which are based on the immunoglobulin structure, antibody mimetics are derived from various protein scaffolds that provide a stable framework for presenting binding sites. These scaffolds include ankyrin repeats, knottins, affibodies, and DARPins (designed

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Electrofusion Technology. Image credit: 10.1002/biot.202200428

Technological Innovations in Antibody Production

The field of antibody production has witnessed significant technological advancements over the past years, particularly in hybridoma technology, which remains a cornerstone for monoclonal antibody (mAb) production. Electrofusion Technology in Hybridoma Preparation Electrofusion technology can be applied as a cell engineering technique for hybridoma preparation. This method offers substantial improvements in efficiency and control over

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VHH-Library-Generation

VHH Library Generation

VHHs, also known as single-domain antibodies or nanobodies, are the smallest antigen-binding fragments derived from heavy-chain-only antibodies found in camelids, such as alpacas, llamas and camels. First discovered in 1993, VHH antibody fragments offer unique characteristics which are particularly advantageous in therapeutics, diagnostics, and research tools. This is due to their small size and structure

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DOI: 10.1038/jid.2013.521

Phage Display Technology

Phage display technology is a powerful technique for antibody discovery. It is often used to identify high-affinity interactions between antibody fragments (e.g. VHHs) and target proteins for the production of monoclonal antibodies. Originally developed in the mid-1980s, phage display is a key technology for antibody engineering, drug discovery, protein-protein interactions, and vaccine development.1 By genetically

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DOI: 10.3389/fmicb.2022.835677

Antibody-Antibiotic Conjugates (AACs) in the Fight Against Bacterial Infections

The rapid rise of antimicrobial resistance (AMR) presents a critical challenge in modern healthcare. Traditional antibiotics are becoming increasingly ineffective against resistant strains of bacteria, necessitating innovative therapeutic strategies. One promising approach is the development of antibody-antibiotic conjugates (AACs). These innovative agents use the selectivity, favorable pharmacokinetics (PK), and safety profile of antibodies, enabling the

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