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Image by Faris Mohammed



Dityrosine (DT) bonds are observed throughout nature in structural proteins such as silk, elastin and collagen where the localized rigidity that DT bonds confer represents a selective advantage with respect to the structural proteins’ strength, toughness and elasticity.


Examples of natural dityrosine crosslinks include human periodontal ligament collagen, aortic elastin, and keratin in skin and hair; structural proteins in plant cell walls; and the cuticles of insects and arthopods.

Dityrosine cross-linking is catalyzed in nature by a diverse group of metallo-enzymes, of which peroxidases are the most prevalent. Calder mimics the natural process of dityrosine crosslink formation, and we therefore use an enzyme that catalyzes the DT cross-linking reaction in nature, while otherwise preserving the structural integrity and functionality of substrate proteins.



In so doing, we successfully harnessed this natural DT cross-linking process and now apply it in a targeted and highly controlled manner, to the design of conformationally-locked vaccine immunogens.

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