Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/47629
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dc.contributor.authorFonseca, Marcela Helena Gambim
dc.contributor.authorFiúza, Tayná da Silva
dc.contributor.authorMorais, Stephanie Bath de
dc.contributor.authorSouza, Tatiana de Arruda Campos Brasil de
dc.contributor.authorTrevizani, Raphael
dc.date.accessioned2021-06-10T19:18:01Z
dc.date.available2021-06-10T19:18:01Z
dc.date.issued2021
dc.identifier.citationFONSECA, Marcela Helena Gambim et al. Circumventing the side effects of L-asparaginase. Biomedicine & Pharmacotherapy, n. 139, p. 1–7, 2021.
dc.identifier.issn0753-3322
dc.identifier.urihttps://www.arca.fiocruz.br/handle/icict/47629
dc.language.isopor
dc.publisherElsevier
dc.rightsopen access
dc.titleCircumventing the side effects of L-asparaginase
dc.typeArticle
dc.identifier.doihttps://doi.org/10.1016/j.biopha.2021.111616
dc.description.abstractenL-asparaginase is an enzyme that catalyzes the degradation of asparagine and successfully used in the treatment of acute lymphoblastic leukemia. L-asparaginase toxicity is either related to hypersensitivity to the foreign protein or to a secondary L-glutaminase activity that causes inhibition of protein synthesis. PEGylated versions have been incorporated into the treatment protocols to reduce immunogenicity and an alternative L-asparaginase derived from Dickeya chrysanthemi is used in patients with anaphylactic reactions to the E. coli L-asparaginase. Alternative approaches commonly explore new sources of the enzyme as well as the use of protein engineering techniques to create less immunogenic, more stable variants with lower L-glutaminase activity. This article reviews the main strategies used to overcome L-asparaginase shortcomings and introduces recent tools that can be used to create therapeutic enzymes with improved features.
dc.creator.affilliationFundação Oswaldo Cruz. Fiocruz Ceará. Eusébio, CE, Brasil.
dc.creator.affilliationNúcleo Multidisciplinar de Bioinformática. BioME, RN, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Fiocruz Ceará. Eusébio, CE, Brasil.
dc.subject.enImmunogenicity
dc.subject.enImmunologic Factors
dc.subject.enL-glutaminase activity
dc.subject.enHalf-Life
dc.subject.enEpitope prediction
dc.subject.enDeimmunization
dc.subject.enProtein Engineering
dc.subject.esFactores Inmunológicos
dc.subject.esGlutaminasa
dc.subject.esSemivida
dc.subject.esMapeo Epitopo
dc.subject.esIngeniería de Proteínas
dc.subject.frFacteurs immunologiques
dc.subject.frPériode
dc.subject.frCartographie épitopique
dc.subject.frIngénierie des protéines
dc.subject.decsFatores Imunológicos
dc.subject.decsGlutaminase
dc.subject.decsMeia-Vida
dc.subject.decsMapeamento de Epitopos
dc.subject.decsEngenharia de Proteínas
Appears in Collections:PR - ICC - Artigos de Periódicos
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