SAH-SOS1A is a KRas/son of sevenless 1 (SOS1) interaction inhibitor. SAH-SOS1A binds within nucleotide binding pocket of KRas (Kd values ranges from 106 - 176 nM for wild type KRas and KRas mutants). SAH-SOS1A inhibits nucleotide binding to KRas in a concentration dependent manner.
CAT No: R1895
CAS No:1652561-87-9
Synonyms/Alias:SAH-SOS1A;1652561-87-9;CRC56187;
Chemical Name:(4S)-4-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S,5S,8S,11S,20S)-20-[[(2S,3S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-5-carbamimidamidopentanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-3-methylpentanoyl]amino]-8-(2-amino-2-oxoethyl)-5-[(1R)-1-hydroxyethyl]-11,20-dimethyl-2-(2-methylpropyl)-3,6,9,21-tetraoxo-1,4,7,10-tetrazacyclohenicos-15-ene-11-carbonyl]amino]-4-methylpentanoyl]amino]-6-aminohexanoyl]amino]-3-hydroxybutanoyl]amino]-4-carboxybutanoyl]amino]-5-[[2-[[(1S)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-5-oxopentanoic acid
SAH-SOS1A is a synthetic peptide inhibitor designed to disrupt the interaction between Son of Sevenless 1 (SOS1) and KRAS, a critical protein-protein interaction in the RAS signaling pathway. As a stabilized alpha-helix of SOS1, this compound mimics a key region of the SOS1 protein, enabling it to competitively bind KRAS and block downstream signaling events. The molecular architecture of SAH-SOS1A incorporates hydrocarbon stapling technology, which enhances its helical stability, proteolytic resistance, and cellular uptake. These features make it an advanced research tool for interrogating RAS-driven cellular processes and for developing targeted strategies in cell signaling studies.
Signal Transduction Research: SAH-SOS1A serves as a valuable molecular probe for dissecting RAS-mediated signal transduction pathways. By specifically inhibiting the SOS1-KRAS interaction, it enables researchers to study the consequences of disrupting RAS activation in various cellular contexts. This targeted approach facilitates the elucidation of downstream effectors, feedback mechanisms, and compensatory pathways activated upon RAS inhibition, thereby advancing understanding of the molecular logic governing cell proliferation, differentiation, and survival.
Protein-Protein Interaction Studies: The peptide's ability to selectively interfere with a well-defined protein-protein interface makes it an effective tool for mapping the structural and functional determinants of the SOS1-KRAS interaction. Researchers can employ it in biochemical assays, such as fluorescence polarization or surface plasmon resonance, to quantify binding affinities and kinetics, or to validate novel binding partners within the RAS interactome. These studies support the rational design of next-generation inhibitors targeting similar protein interfaces.
Chemical Biology and Probe Development: As a prototype stapled peptide, SAH-SOS1A exemplifies the utility of hydrocarbon stapling for generating bioactive, cell-permeable research probes. Its use informs the development of other stabilized peptides aimed at modulating intracellular targets that are traditionally considered "undruggable." In chemical biology, the compound is employed to investigate the cellular consequences of acute, selective disruption of protein-protein contacts, providing mechanistic insights that are otherwise difficult to achieve with genetic or small-molecule approaches.
Cellular Pathway Modulation: In cell-based assays, SAH-SOS1A is utilized to transiently inhibit RAS signaling, enabling functional studies of pathway dynamics and cellular phenotypes resulting from acute pathway suppression. Such experiments are critical for identifying context-dependent vulnerabilities, adaptive responses, and potential synthetic lethal interactions that arise upon RAS pathway blockade. The peptide's cell-penetrating properties further allow for its application in diverse cell lines and primary cell models.
Peptide Engineering and Method Development: The design and application of SAH-SOS1A have contributed to advances in the field of peptide engineering. Its hydrocarbon-stapled structure demonstrates strategies for enhancing peptide drug-like properties, such as secondary structure stabilization and protease resistance. Researchers leverage it as a model system for optimizing stapling methodologies, evaluating peptide bioactivity, and benchmarking new approaches to the synthesis and delivery of functional peptides in cellular environments.
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