Direct Comparison of Label-Free Biosensor Binding Kinetics Obtained on the Biacore 8K and the Carterra LSA

• Published in: SLAS discovery Vol. 25; no. 9; pp. 977 - 984
• Main Authors: Knowling, Stuart, Clark, Jennifer, Sjuts, Hanno, Abdiche, Yasmina Noubia
• Format: Journal Article
• Language: English
• Published: Los Angeles, CA SAGE Publications 01.10.2020
• Subjects: protein–protein interactions; antibody; antibody arrays; cancer and cancer drugs; large-molecule therapeutics
• ISSN: 2472-5552; 2472-5560
• DOI: 10.1177/2472555220934814

Funding pressure on the pharmaceutical industry to deliver new medicines to the market under aggressive timelines has led to a demand for analytical tools with higher detection sensitivity, increased throughput, and automation to speed up research and discovery efforts and converge upon clinically fit leads faster. In the quest for therapeutic antibodies, the early adoption of interaction analysis platforms utilizing surface plasmon resonance (SPR) detection provides insightful molecular-level information about the binding properties of antibody libraries that are key to understanding an antibody’s mechanism of action and can guide the library-to-leads triage. Here, we sought to compare the binding kinetics obtained on two state-of-the-art high-throughput SPR platforms in an independent study conducted by unrelated groups located on different continents. We show that when experiments were performed by skilled users adhering to SPR best practices and allowed freedom in their assay design, the two platforms yielded near-identical results, establishing them both as reliable tools in accelerating the characterization of antibody libraries in providing critical information needed to advance leads to the clinic.