Coupling Strategies of Immuno-toxin

Introduction of Immunotoxin Conjugation

Immunotoxin conjugation is a complex process that requires careful consideration of the linker design and conjugation technologies to obtain an effective and selective therapeutic agent for targeted cancer therapy and other diseases. Various types of linkers can be used in immunotoxin conjugation, including cleavable linkers such as disulfide bonds, peptide linkers that can be cleaved by proteases, or non-cleavable linkers that rely on internalization of the conjugate into the target cell to release the toxin. The choice of linker depends on factors such as the toxin molecule, desired payload release mechanism, and target cell characteristics. At Creative Biolabs, our team is dedicated to providing customized immunotoxin conjugates with optimal stability, potency, and selectivity. Our cutting-edge technologies and extensive experience in the field ensure that you will receive the highest quality immunotoxin conjugates tailored to achieve successful research.

Fig.1 Three generations of immunotoxins. (Shapira & Itai, 2010)Fig.1 Three generations of immunotoxins.1

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The choice of linker used in immunotoxin conjugation is critical, as it can significantly impact the stability, potency, and selectivity of the resultant immunotoxin. At Creative Biolabs, we provide several conjugation technologies for immunotoxin construction. Our expertise enables us to offer a wide range of conjugation methods tailored to deliver optimal immunotoxin properties.

Toxins can be conjugated to the targeting moieties through non-specific chemical methods, such as maleimide-thiol or NHS-amine reactions. Our expertise in chemical conjugation enables us to manipulate molecules with high precision and control, ensuring optimal immunotoxin performance.

Site-specific conjugation of immunotoxins involves attaching a chemical linker to a specific amino acid residue on the immunotoxin molecule. The DNA sequence encoding the immunotoxin is modified to introduce a specific amino acid residue or a reactive group at a desired site. The modified functional groups on the immunotoxin can then be reacted with specific reactive groups such as maleimide, NHS ester, or azide, resulting in site-specific conjugation.

The fusion immunotoxins are typically generated using recombinant DNA technology, where the gene encoding the targeting domain is fused with the gene encoding the toxin moiety, connected by a linker sequence. The peptide linker serves as a flexible spacer that allows for the proper folding of the fusion protein and maintains the functional integrity of both the targeting domain and the toxin moiety. This fusion gene is then expressed in a suitable expression system, such as bacteria, yeast, or mammalian cells, to produce the final fusion immunotoxin protein.

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Reference

  1. Shapira, Assaf, and Itai Benhar. "Toxin-based therapeutic approaches." Toxins 2.11 (2010): 2519-2583.

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