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The study aims to analyze how secondary mutations in KRAS-G12C affect the efficacy of covalent inhibitors.

Abstract B002: Structural and functional analysis of the resistance mechanisms of KRAS-G12C secondary mutations to switch-II pocket inhibitors

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The study aims to analyze how secondary mutations in KRAS-G12C affect the efficacy of covalent inhibitors.
Characterization of KRAS secondary mutations using structural biology and molecular dynamics.
Biochemical assays to measure Kinact/Ki parameters for various inhibitors.
Cellular analyses to evaluate downstream signaling pathways and effector interactions.
High-resolution crystal structures show mutation-specific changes in the Switch-II pocket.
Molecular dynamics indicate altered flexibility affecting inhibitor binding.
Distinct reductions in covalent engagement observed for each inhibitor across the resistance panel.

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Reveals the structural impacts of KRAS-G12C secondary mutations on inhibitor efficacy, suggesting new therapeutic strategies.

Whitley et al. (2026) studied this question.

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