Peptide-MHC I complex stability measured by nanoscale differential scanning fluorimetry reveals molecular mechanism of thermal denaturation

August 31, 2021

Saikia, A. and Springer, S.

Molecular Immunology 2021, vol: 136 doi: 10.1016/j.molimm.2021.04.028

Abstract

Recombinant major histocompatibility complex class I molecules are used in diagnostic and therapeutic approaches in cancer immunotherapy, with many studies exploring their binding to antigenic peptides. Current techniques for kinetic peptide binding studies are hampered by high sample consumption, low throughput, interference with protein stability, and/or high background signal. Here, we validate nanoscale differential scanning fluorimetry (nanoDSF), a method using the tryptophan fluorescence of class I molecules, for class I/peptide binding, and we use it to determine the molecular mechanism of the thermal denaturation of HLA-A*02:01.

View Publication

Topics: Prometheus, nanoDSF, Biologics, Publications

Previous Video
Use of high-throughput methods for early stage formulation evaluation and their correlation to stability studies
Use of high-throughput methods for early stage formulation evaluation and their correlation to stability studies

AbbVie preformulation is an early discovery biologics group working to optimise antibodies prior to downstr...

Up next
Rapid and precise biosimilar candidate profiling by nanoDSF
Rapid and precise biosimilar candidate profiling by nanoDSF

Looking for the optimal formulation for your biologics candidates?

NanoTemper tools can help

Find out how