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    Wyświetlanie 1-9 z 9
    Tytuł:
    Reengineering of an artificial protein cage for efficient packaging of active enzymes
    Autorzy:
    Pasternak, Monika
    Azuma, Yusuke
    Barczyk-Woźnicka, Olga
    Pyza, Elżbieta
    Heddle, Jonathan
    Gaweł, Szymon
    Opis:
    Protein cages that readily encapsulate active enzymes of interest present useful nanotools for delivery and catalysis, wherein those with programmable disassembly characteristics serve as particularly attractive platforms. Here, a general guest packaging system based on an artificial protein cage, TRAP‐cage, the disassembly of which can be induced by the addition of reducing agents, is established. In this system, TRAP‐cage with SpyCatcher moieties in the lumen is prepared using genetic modification of the protein building block and assembled into a cage structure with either monovalent gold ions or molecular crosslinkers. The resulting protein cage can efficiently capture guest proteins equipped with a SpyTag by simply mixing them in an aqueous solution. This post‐assembly loading system, which circumvents the exposure of guests to thiol‐reactive crosslinkers, enables the packaging of enzymes possessing a catalytic cysteine or a metal cofactor while retaining their catalytic activity.
    Dostawca treści:
    Repozytorium Uniwersytetu Jagiellońskiego
    Artykuł
    Tytuł:
    Designed, programmable protein cages utilizing diverse metal coordination geometries show reversible, pH-dependent assembly
    Autorzy:
    Azuma, Yusuke
    Heddle, Jonathan G.
    Pakosz‐Stępień, Zuzanna
    Biela, Artur
    Majsterkiewicz, Karolina
    Osiński, Norbert
    Gaweł, Szymon
    Opis:
    The rational design and production of a novel series of engineered protein cages are presented, which have emerged as versatile and adaptable platforms with significant applications in biomedicine. These protein cages are assembled from multiple protein subunits, and precise control over their interactions is crucial for regulating assembly and disassembly, such as the on‐demand release of encapsulated therapeutic agents. This approach employs a homo‐undecameric, ring‐shaped protein scaffold with strategically positioned metal binding sites. These engineered proteins can self‐assemble into highly stable cages in the presence of cobalt or zinc ions. Furthermore, the cages can be disassembled on demand by employing external triggers such as chelating agents and changes in pH. Interestingly, for certain triggers, the disassembly process is reversible, allowing the cages to reassemble upon reversal or outcompeting of triggering conditions/agents. This work offers a promising platform for the development of advanced drug delivery systems and other biomedical applications
    Dostawca treści:
    Repozytorium Uniwersytetu Jagiellońskiego
    Artykuł
    Tytuł:
    Encapsidic production and isolation of degradation-prone polypeptides
    Autorzy:
    Kwaśna, Dominika
    Koziej, Łukasz
    Pankowski, Jędrzej
    Kachamakova-Trojanowska, Neli
    Zarechyntsava, Maria
    Klóska, Damian
    Gawin-Grębla, Agnieszka
    Azuma, Yusuke
    Glatt, Sebastian
    Opis:
    Degradation during production and delivery is a significant bottleneck in developing biomolecular therapies. Protein cages, formed by engineered variants of lumazine synthase, present an effective strategy for the microbial production and isolation of labile biomolecular therapies. Genetic fusion of the target polypeptide to a cage component protomer ensures its efficient encapsulation within the cage during production in host bacterial cells, thereby protecting it from degradation. Furthermore, controlled cage opening outside the cellular environment facilitates the isolation of the encapsulated cargo through sequence-specific protease cleavage. Notably, the system features a modular patchwork assembly to prevent guest overloading, avoiding unwanted incomplete cage formation and insoluble aggregates. The broad applicability of the “encapsidic” approach is demonstrated by the efficient production of six distinct, intrinsically disordered polypeptides with proven therapeutic potential.
    Dostawca treści:
    Repozytorium Uniwersytetu Jagiellońskiego
    Artykuł
      Wyświetlanie 1-9 z 9

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