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ASP-Enzymosomes with Saccharomyces cerevisiae Asparaginase II Expressed in Pichia pastoris : Formulation Design and In Vitro Studies of a Potential Antileukemic Drug

Girão, Luciana F C ; Carvalheiro, Manuela Colla ; Ferreira-Silva, Margarida ; da Rocha, Surza L G ; Perales, Jonas ; Martins, M Bárbara F ; Ferrara, Maria Antonieta ; Bon, Elba P S ; Corvo, M Luísa

International journal of molecular sciences, 2021-10, Vol.22 (20), p.11120 [Periódico revisado por pares]

Switzerland: MDPI AG

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Título:
ASP-Enzymosomes with Saccharomyces cerevisiae Asparaginase II Expressed in Pichia pastoris : Formulation Design and In Vitro Studies of a Potential Antileukemic Drug
Autor: Girão, Luciana F C ; Carvalheiro, Manuela Colla ; Ferreira-Silva, Margarida ; da Rocha, Surza L G ; Perales, Jonas ; Martins, M Bárbara F ; Ferrara, Maria Antonieta ; Bon, Elba P S ; Corvo, M Luísa
Assuntos: Acute lymphoblastic leukemia ; Amino acids ; Antineoplastic Agents - chemistry ; Antineoplastic Agents - metabolism ; Antineoplastic Agents - pharmacology ; Antiproliferatives ; ASP-enzymosomes ; ASP3 gene ; Asparaginase ; Asparaginase - chemistry ; Asparaginase - genetics ; Asparaginase - metabolism ; Asparaginase - pharmacology ; Chromatography ; Chronic myeloid leukemia ; Drug Compounding - methods ; Drug Design ; Drug development ; Drug Screening Assays, Antitumor ; E coli ; enzymatic therapy ; Enzymes ; Fungi ; Glutaminase ; Humans ; Immunology ; Jurkat Cells ; K562 Cells ; Leukemia ; Leukemia - drug therapy ; Leukemia - pathology ; leukemia treatment ; Lipids ; Liposomes ; Lymphatic leukemia ; Myeloid leukemia ; nanoformulations ; Nanoparticles ; Pichia pastoris ; Polyethylene glycol ; Polymers ; Proteins ; Reagents ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomycetales - genetics ; Saccharomycetales - metabolism ; Tumor cell lines ; Tumor Cells, Cultured ; Yeast ; yeast asparaginase
É parte de: International journal of molecular sciences, 2021-10, Vol.22 (20), p.11120
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SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: The bacterial enzyme asparaginase is the main treatment option for acute lymphoblastic leukemia. However, it causes side effects, such as immunological reactions, and presents undesirable glutaminase activity. As an alternative, we have been studying asparaginase II from , coded by gene, which was cloned and expressed in The recombinant asparaginase (ASP) presented antileukemic activity and a glutaminase activity 100 times lower in comparison to its asparaginase activity. In this work, we describe the development of a delivery system for ASP via its covalent attachment to functionalized polyethylene glycol (PEG) polymer chains in the outer surface of liposomes (ASP-enzymosomes). This new delivery system demonstrated antiproliferative activity against K562 (chronic myeloid leukemia) and Jurkat (acute lymphocytic leukemia) cell lines similar to that of ASP. The antiproliferative response of the ASP-enzymosomes against the Jurkat cells suggests equivalence to that of the free commercial asparaginase (Aginasa ). Moreover, the ASP-enzymosomes were stable at 4 °C with no significant loss of activity within 4 days and retained 82% activity up to 37 days. Therefore, ASP-enzymosomes are a promising antileukemic drug.
Editor: Switzerland: MDPI AG
Idioma: Inglês

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ASP-Enzymosomes with Saccharomyces cerevisiae Asparaginase II Expressed in Pichia pastoris : Formulation Design and In Vitro Studies of a Potential Antileukemic Drug

Girão, Luciana F C ; Carvalheiro, Manuela Colla ; Ferreira-Silva, Margarida ; da Rocha, Surza L G ; Perales, Jonas ; Martins, M Bárbara F ; Ferrara, Maria Antonieta ; Bon, Elba P S ; Corvo, M Luísa

Switzerland: MDPI AG

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