KRAS-related Assays: Binding kinetics of agents to K-Ras are measured via surface plasmon resonance (SPR) technique
K-Ras
KRAS
K-Ras fragments aa 2-169 with a C-terminal biotinylation expressed in E. coli. Data shown here was collected for KRAS in a GDP-bound state.
C-K-RAS, CFC2, K-RAS2A, K-RAS2B, K-RAS4A, K-RAS4B, KI-RAS, KRAS1, KRAS2, NS, NS3, RASK2
K-Ras: P01116 (https://www.uniprot.org/uniprot/P01116)
Small molecule and peptide binding to KRAS wildtype and mutants.
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Binding kinetics of KRpep-2d to wild type K-Ras and mutants G12C, G12D, G12V, and G12R
The data was collected on a Biacore 8K using single-cycle kinetics. The data was fit using a 1:1 kinetic binding model. The peptide binds with the tightest affinity to K-Ras mutant G12D.
Binding kinetics of BI-2852 to wild type K-Ras and mutants G12C, G12D, G12V, G12R, and double mutant G12D/T35S
The data was collected on a Biacore 8K using multi-cycle kinetics. The data was fit using a 1:1 kinetic binding model. BI-2852 binds to all KRAS constructs with similar kinetics/affinity.
Binding kinetics of MRTX1133 to wild type K-Ras and mutants G12C, G12D, and G12V
The data was collected on a Biacore 8K using single-cycle kinetics. The data was fit using a 1:1 kinetic binding model. While MRTX1133 exhibits relatively tight binding to all the KRAS constructs tested, the off-rate is significantly slower for binding to KRAS G12D resulting in an KD value that is at least an order of magnitude tighter than for the other constructs.