TECHNICAL
NOTE
Better optimization of biosensor assay development with
Tycho™ NT.6
Dennis Breitsprecher and Nuska Tschammer
NanoTemper Technologies GmbH, Floessergasse 4, 81369 Munich
Abstract
Surface plasmon resonance (SPR) is an optical methodology used to detect and
quantify molecular interactions. Although SPR is widely used and considered by
many researchers to be the gold standard for quantification of protein interactions,
assay optimization can be technically challenging, time-consuming and costly.
The Tycho NT.6 system quickly analyzes different conditions typically tested when
optimizing an SPR assay. It utilizes very small amounts of sample and provides
dramatic time and cost savings compared to standard SPR assay development
procedures. Tycho NT.6 is simple to use and enables researchers to make better
educated decisions in developing and optimizing their binding interaction assays.
Introduction
Surface plasmon resonance (SPR) and other biosensor-based analytical
methods are standard tools used in academic and pharmaceutical research
laboratories for the quantification of protein interactions. Typically, one binding
partner – the ligand – is covalently immobilized on the surface of a biosensor
chip, while the other binding partner – the analyte – is added in solution to
measure binding kinetics. Covalent immobilization of proteins to the biosensor
surface is o en problematic, since acidic, salt-free buffers are required for
optimal coupling using lysine chemistry. These harsh conditions can negatively
influence protein integrity and function.
