Open AccessFrom Synthesis to Characterization of Site-Selective PEGylated Proteins
Author(s) -
Lisandra Herrera Belén,
Carlota de Oliveira RangelYagui,
Jorge Félix Beltrán Lissabet,
Brian Effer,
Manuel LeeEstévez,
Adalberto Pessoa,
Rodrigo L. Castillo,
Jorge G. Farías
Publication year - 2019
Publication title -
frontiers in pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.384
H-Index - 86
ISSN - 1663-9812
DOI - 10.3389/fphar.2019.01450
Subject(s) - pegylation , polyethylene glycol , peg ratio , reactogenicity , chemistry , combinatorial chemistry , residue (chemistry) , amino acid residue , covalent bond , biochemistry , computational biology , nanotechnology , materials science , peptide sequence , immunogenicity , organic chemistry , biology , gene , immunology , economics , immune system , finance
Covalent 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.
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