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From synthesis to characterization of site-selective pegylated proteins

dc.contributor.authorBelén L.H.
dc.contributor.authorDe Oliveira Rangel-Yagui C.
dc.contributor.authorBeltrán Lissabet J.F.
dc.contributor.authorEffer B.
dc.contributor.authorLee-Estevez M.
dc.contributor.authorPessoa A.
dc.contributor.authorCastillo R.L.
dc.contributor.authorFarías J.G.
dc.date.accessioned2020-09-02T22:13:05Z
dc.date.available2020-09-02T22:13:05Z
dc.date.issued2019
dc.identifier10.3389/fphar.2019.01450
dc.identifier.citation10, , -
dc.identifier.issn16639812
dc.identifier.urihttps://hdl.handle.net/20.500.12728/3728
dc.descriptionCovalent attachment of therapeutic proteins to polyethylene glycol (PEG) is widely used for the improvement of its pharmacokinetic and pharmacological properties, as well as the reduction in reactogenicity and related side effects. This technique named PEGylation has been successfully employed in several approved drugs to treat various diseases, even cancer. Some methods have been developed to obtain PEGylated proteins, both in multiple protein sites or in a selected amino acid residue. This review focuses mainly on traditional and novel examples of chemical and enzymatic methods for site-selective PEGylation, emphasizing in N-terminal PEGylation, that make it possible to obtain products with a high degree of homogeneity and preserve bioactivity. In addition, the main assay methods that can be applied for the characterization of PEGylated molecules in complex biological samples are also summarized in this paper. Copyright © 2019 Belén, Rangel-Yagui, Beltrán Lissabet, Effer, Lee-Estevez, Pessoa, Castillo and Farías. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
dc.language.isoen
dc.publisherFrontiers Media S.A.
dc.subjectCharacterization
dc.subjectEnzymatic ligation
dc.subjectN-terminal PEGylation
dc.subjectProtein PEGylation
dc.subjectSite-selective conjugation
dc.subjectbutelase 1
dc.subjectcysteine
dc.subjectligase
dc.subjectlipoid acid ligase
dc.subjectprotein glutamine gamma glutamyltransferase
dc.subjectserine
dc.subjectsubtiligase
dc.subjectthreonine
dc.subjecttryptophan
dc.subjecttyrosine
dc.subjectunclassified drug
dc.subjectamino terminal sequence
dc.subjectbioinformatics
dc.subjectbiological activity
dc.subjectclick chemistry
dc.subjectcomplex formation
dc.subjectconjugation
dc.subjectcovalent bond
dc.subjectenzyme immunoassay
dc.subjecthigh performance liquid chromatography
dc.subjectmass spectrometry
dc.subjectPEGylation
dc.subjectphoton correlation spectroscopy
dc.subjectphysical chemistry
dc.subjectprotein determination
dc.subjectprotein expression
dc.subjectprotein polymerization
dc.subjectprotein synthesis
dc.subjectprotein targeting
dc.subjectproton nuclear magnetic resonance
dc.subjectReview
dc.titleFrom synthesis to characterization of site-selective pegylated proteins
dc.typeReview


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