A short peptide fragment of the vascular endothelial growth factor as a novel ligand for bevacizumab purification.
Animals
Antineoplastic Agents
/ chemistry
Bevacizumab
/ chemistry
CHO Cells
/ metabolism
Chemistry, Pharmaceutical
Chromatography, Affinity
Cricetulus
Drug Stability
Humans
Immobilized Proteins
Ligands
Peptide Fragments
/ chemistry
Protein Binding
Sepharose
/ chemistry
Surface Properties
Vascular Endothelial Growth Factor A
/ chemistry
Affinity chromatography
Monoclonal antibodies
Purification
Short peptide
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
01 2020
01 2020
Historique:
received:
26
07
2019
revised:
10
09
2019
accepted:
17
09
2019
pubmed:
23
9
2019
medline:
19
12
2020
entrez:
23
9
2019
Statut:
ppublish
Résumé
Bevacizumab is a vascular endothelial growth factor (VEGF)-directed monoclonal antibody (mAb) used for the treatment of several human cancers. Given that bevacizumab is administered intravenously, it must have extremely high purity, which is achieved by purification with protein A affinity chromatography (AC). However, protein A is a very expensive ligand, thereby increasing the cost of purification. Furthermore, the harsh elution conditions required to recover bevacizumab from the AC column can damage both the mAb and protein A. In contrast, short peptides show higher stability, easier synthesis and lower cost and are therefore ideal ligands for AC. In the present study, the peptide Ac-PHQGQHIGVSK contained in the VEGF fragment that binds bevacizumab, was synthesized and immobilized on agarose. The peptidyl-agarose showed affinity for bevacizumab, with an equilibrium dissociation constant value of 2.2±0.5 x 10
Identifiants
pubmed: 31542564
pii: S1046-5928(19)30386-9
doi: 10.1016/j.pep.2019.105500
pii:
doi:
Substances chimiques
Antineoplastic Agents
0
Immobilized Proteins
0
Ligands
0
Peptide Fragments
0
Vascular Endothelial Growth Factor A
0
Bevacizumab
2S9ZZM9Q9V
Sepharose
9012-36-6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
105500Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.