Characterization of PEGylated Asparaginase: New Opportunities from NMR Analysis of Large PEGylated Therapeutics.
PEGylation
biopharmaceuticals
protein modifications
protein structures
structural biology
Journal
Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783
Informations de publication
Date de publication:
06 Feb 2019
06 Feb 2019
Historique:
received:
03
09
2018
revised:
09
11
2018
pubmed:
22
11
2018
medline:
1
8
2019
entrez:
22
11
2018
Statut:
ppublish
Résumé
Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography.
Identifiants
pubmed: 30462348
doi: 10.1002/chem.201804488
doi:
Substances chimiques
Coated Materials, Biocompatible
0
Polyethylene Glycols
3WJQ0SDW1A
Asparaginase
EC 3.5.1.1
Types de publication
Journal Article
Langues
eng
Pagination
1984-1991Subventions
Organisme : European Commission
ID : 261572
Organisme : European Commission
ID : 675858
Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.