The immunogenicity of an anti-EGFR single domain antibody (V
Animals
Antibodies
/ immunology
Antibody Formation
/ immunology
ErbB Receptors
/ immunology
Escherichia coli
/ immunology
Female
Hot Temperature
Mice
Mice, Inbred ICR
Protein Aggregates
/ immunology
Protein Aggregation, Pathological
/ immunology
Protein Folding
Single-Domain Antibodies
/ immunology
Solubility
Amorphous aggregation
Anti-drug antibodies
Disulfide bond
Immunogenicity
Protein aggregation
Protein misfolding
Protein solubility
SS bond
Single domain antibody
Journal
European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V
ISSN: 1873-3441
Titre abrégé: Eur J Pharm Biopharm
Pays: Netherlands
ID NLM: 9109778
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
received:
12
02
2020
revised:
07
05
2020
accepted:
10
05
2020
pubmed:
18
5
2020
medline:
7
2
2021
entrez:
17
5
2020
Statut:
ppublish
Résumé
Amorphous aggregates of therapeutic proteins can provoke an unwanted immune response (anti-drug antibodies; ADAs), but counter-examples have led to some controversy. Amorphous aggregates can possess unique biophysical and biochemical attributes depending on both the way they are generated and the protein's biophysical/biochemical properties. Here, we examine the immunogenicity of an anti-EGFR single domain antibody (V
Identifiants
pubmed: 32416134
pii: S0939-6411(20)30134-X
doi: 10.1016/j.ejpb.2020.05.006
pii:
doi:
Substances chimiques
Antibodies
0
Protein Aggregates
0
Single-Domain Antibodies
0
EGFR protein, mouse
EC 2.7.10.1
ErbB Receptors
EC 2.7.10.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
164-174Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.