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The prototypic compound KRpep-2d blocks the interaction between KRAS and SOS1, thereby preventing nucleotide exchange and downstream RAFMEKERK activation.61 Subsequent chemical optimisation, including hydrocarbon stapling and arginine-rich linkers, has improved membrane permeability and metabolic stability, leading to measurable suppression of pERK signalling in KRAS-G12D -mutant cell lines.62 Further derivatives, such as cyclorasin and LYRAS analogues, extend activity across KRAS-G12D and KRAS-G12V mutants by disrupting RASeffector interactions and inducing tumour regression in preclinical xenografts.63 Although challenges remain in enhancing intracellular delivery and systemic stability, these macrocyclic peptides demonstrate that even undruggable KRAS alleles possess tractable binding surfaces, offering a conceptual bridge between small-molecule inhibitors and biologic therapeutics

E., & Hare, J

References: Beutler E, Felitti VJ, Gelbart T, Ho N

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