Pieris successfully demonstrates proprietary biotherapeutics platform: Dual targeting with Duocalin technology
Pieris AG announced that its proprietary Duocalin® technology has successfully demonstrated dual targeting potential. Commenting on this development, Dr Andreas Hohlbaum, Director of Science and Preclinical Development of Pieris said: "As Pieris continues to validate the therapeutic application of its technologies, dual targeting is viewed as a major step forward. Combining the benefits of bivalent, avid binding of disease targets with the ability to modulate two targets at once shows the clear development potential of the Duocalin® technology to treat multi-factorial diseases".
Using individual monomeric Anticalins® selected to have picomolar binding affinity to distinct determinants on two defined clinically validated targets, Pieris has constructed Duocalins® as monomeric, bivalent binding proteins that retain target specificity and affinity regardless of the structural orientation of their binding domains. Furthermore, the high intrinsic stability of Duocalins® is comparable to monomeric Anticalins®, offering flexible formulation and delivery potential for Duocalin®-based drug candidates.
Despite the low molecular weight of monomeric Anticalins® relative to antibodies, their core scaffold provides a highly selective binding site with high structural plasticity and an extensive binding surface comparable to that achieved with antibodies. The adaptability of the Anticalin® scaffold has already allowed Pieris to develop therapeutic and diagnostic product candidates with custom designed functionality. Duocalins® allow multiple targets to be bound and modulated through a single molecule, which is particularly advantageous in diseases known to involve more than a single causative factor. Moreover, bi- or multivalent binding formats such as Duocalins® have significant potential in targeting cell surface molecules in disease, mediating agonistic effects on signal transduction pathways or inducing enhanced internalization effects via binding and clustering of cell surface receptors.
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