T lymphocytes display a remarkable ability to evaluate differences in MHC-peptide complexes. Alteration of a single amino acid in an antigenic peptide has significant and distinct biological effects on the T cell recognition. Current research proposes all these events are governed by the TCR-MHC interactions. Using well developed micropipette and confocal microscope techniques, as well as relative cellular and mouse model, specific experiments are being conducted to find the common mechanism of the TCR-MHC interaction by quantitatively measuring the binding kinetics and comparing with corresponding biological effects, thereby providing a basis for rational design of immunotherapy.
AFM on which the cantilever works horizontally (parallel to the earth); can measure receptor-ligand binding kinetics under force on live cells
|Title||First Author||Journal||Date||PMID||DOI||More Information|
|Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell||Yunfeng Chen||J Vis Exp.||8/4/2015||26274371||10.3791/52975||More Info|
|Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics||Lining Ju||Thromb Res||6/20/2015||None||10.1016/j.thromres.2015.06.019||More Info|
|Direct observation of catch bonds involving cell-adhesion molecules||Marshall BT||Nature||5/8/2003||12736689||10.1038/nature01605||More Info|