Causes of Industrial Protein A Column Degradation, Explored Using Raman Spectroscopy.
Journal
Analytical chemistry
ISSN: 1520-6882
Titre abrégé: Anal Chem
Pays: United States
ID NLM: 0370536
Informations de publication
Date de publication:
15 11 2022
15 11 2022
Historique:
pubmed:
2
11
2022
medline:
18
11
2022
entrez:
1
11
2022
Statut:
ppublish
Résumé
Monoclonal antibodies (mAbs) are used extensively as biotherapeutics for chronic and acute conditions. Production of mAbs is lengthy and expensive, with protein A affinity capture the most costly step, due both to the nature of the resin and its marked reduction in binding capacity with repeated use. Our previous studies using in situ ATR-FTIR spectroscopy indicated that loss in protein A binding capacity is not the result of leaching or degradation of protein A ligand, suggesting fouling is the principal cause. Here we explore binding behavior and resin capacity loss using Raman spectroscopy. Our data reveal a distinct Raman spectral fingerprint for mAb bound to the protein A ligand of MabSelect SuRe. The results show that the drop in static binding capacity (SBC) previously observed for used protein A resin is discernible by Raman spectroscopy in combination with partial least-squares regression. The SBC is lowest (35.76 mg mL
Identifiants
pubmed: 36318727
doi: 10.1021/acs.analchem.2c03063
pmc: PMC9670029
doi:
Substances chimiques
Staphylococcal Protein A
0
Ligands
0
Antibodies, Monoclonal
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
15703-15710Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R019533/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/S506965/1
Pays : United Kingdom
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