title: Glycan characterization of biopharmaceuticals: Updates and perspectives.
abstract: Therapeutic proteins are rapidly becoming the most promising class of pharmaceuticals on the market due to their successful treatment of a vast array of serious diseases, such as cancers and immune disorders. Therapeutic proteins are produced using recombinant DNA technology. More than 60% of therapeutic proteins are posttranslationally modified following biosynthesis by the addition of N- or O-linked glycans. Glycosylation is the most common posttranslational modifications of proteins. However, it is also the most demanding and complex posttranslational modification from the analytical point of view. Moreover, research has shown that glycosylation significantly impacts stability, half-life, mechanism of action and safety of a therapeutic protein. Considering the exponential growth of biotherapeutics, this present review of the literature (2009-2015) focuses on the characterization of protein glycosylation, which has witnessed an improvement in methodology. Furthermore, it discusses current issues in the fields of production and characterization of therapeutic proteins. This review also highlights the problem of non-standard requirements for the approval of biosimilars with regard to their glycosylation and discusses recent developments and perspectives for improved glycan characterization.
authors.affiliation: Analytical Platform of the Faculty of Pharmacy and Laboratory of Pharmaceutical Chemistry, Faculty of Pharmacy, Universite Libre de Bruxelles (ULB), Brussels, Belgium.
authors.forename: Ana
authors.initials: A
authors.lastname: Planinc
authors.affiliation: Characterisation and Comparability Laboratory, NIBRT - The National Institute for Bioprocessing Research and Training, Foster Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland.
authors.forename: Jonathan
authors.initials: J
authors.lastname: Bones
authors.affiliation: Laboratory of Instrumental Analysis and Bioelectrochemistry, Faculty of Pharmacy, Université Libre de Bruxelles (ULB), Boulevard du Triomphe, B-1050 Brussels, Belgium; Department of Analytical Chemistry and Pharmaceutical Technology (FABI), Center for Pharmaceutical Research (CePhaR), Faculty of Medicines and Pharmacy, Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, B-1090 Brussels, Belgium.
authors.forename: Bieke
authors.initials: B
authors.lastname: Dejaegher
authors.affiliation: Analytical Platform of the Faculty of Pharmacy and Laboratory of Pharmaceutical Chemistry, Faculty of Pharmacy, Universite Libre de Bruxelles (ULB), Brussels, Belgium.
authors.forename: Pierre
authors.initials: P
authors.lastname: Van Antwerpen
authors.affiliation: Analytical Platform of the Faculty of Pharmacy and Laboratory of Pharmaceutical Chemistry, Faculty of Pharmacy, Universite Libre de Bruxelles (ULB), Brussels, Belgium. Electronic address: cedric.delporte@ulb.ac.be.
authors.forename: Cédric
authors.initials: C
authors.lastname: Delporte
mesh_terms: D000818:Animals; D059451:Biosimilar Pharmaceuticals / Q000737:chemistry*; D002623:Chemistry Techniques, Analytical / Q000379:methods; D006031:Glycosylation; D006801:Humans; D011134:Polysaccharides / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D059451:Biosimilar Pharmaceuticals; D011134:Polysaccharides; D011506:Proteins; D011994:Recombinant Proteins
keywords: Bioinformatics; Biopharmaceuticals; Biosimilars; Glycan analysis guidelines; Glycan detection; Glycan separation; N-glycosylation