l-Asparaginase In Situ Encapsulated into Zwitterionic Nanocapsules with a Prolonged Half-Life AITranslate

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DOI：https://doi.org/10.1021/acsapm.2c00068

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The heterologous origin of the enzyme usually induces some unwanted enzyme-related complications including immunological responses and decreased plasma half-life, which limits its greater therapeutic effects and applications in patients. Poly(zwitterion) offers a promising opportunity to evolve a generation of nanoparticles with their huge potential to prevent the nonspecific adsorption of biomolecules and enormous capacity to preserve the circulation half-lives and divert the recognition of the mononuclear phagocytic system. In this study, we encapsulated the l-asparaginase enzyme in superbiocompatible phosphorylcholine polymer shells, forming a zwitterion-coated enzyme nanocapsule. This formulated structure presents the encapsulated enzyme with an improved stability against proteolysis, extended half-life in vivo, and lower immunogenicity after repeated treatments. Such nanocapsules along with these improved characteristics propose an alternative delivery platform for l-asparaginase to break through the previous limitations and translate more efficiently to clinical applications. The demonstrated technology presents a suitable approach for enzyme delivery, but it can also be used to encapsulate the emerging classes of protein therapeutics, bioimaging agents, and biosensors.