MM-102 is a novel potent inhibitor of MLL1/WDR5 protein-protein interaction.
CAT No: R1919
CAS No:1417329-24-8
Synonyms/Alias:MM-102;1417329-24-8;HMTase Inhibitor IX;N-[bis(4-fluorophenyl)methyl]-1-[[(2S)-5-(diaminomethylideneamino)-2-[[2-ethyl-2-(2-methylpropanoylamino)butanoyl]amino]pentanoyl]amino]cyclopentane-1-carboxamide;CHEMBL3883592;SCHEMBL12035529;BDBM200723;MM102;(S)-N-(Bis(4-fluorophenyl)methyl)-1-(2-(2-ethyl-2-isobutyramidobutanamido)-5-guanidinopentanamido)cyclopentanecarboxamide;BCP11764;EX-A1503;s7265;AKOS030526507;CCG-270356;MM-102?;NCGC00351775-01;AC-36316;DA-65547;HY-12220;TS-09297;US9233086, 10L;SW220028-1;G14355;BRD-K68474068-001-01-8;cyclopentanecarboxamide, 1-[[(2S)-5-[(aminoiminomethyl)amino]-2-[[2-ethyl-2-[(2-methyl-1-oxopropyl)amino]-1-oxobutyl]amino]-1-oxopentyl]amino]-N-[bis(4-fluorophenyl)methyl]-;N-[bis(4-fluorophenyl)methyl]-1-[(2S)-5-carbamimidamido-2-[2-ethyl-2-(2-methylpropanamido)butanamido]pentanamido]cyclopentane-1-carboxamide;
Chemical Name:N-[bis(4-fluorophenyl)methyl]-1-[[(2S)-5-(diaminomethylideneamino)-2-[[2-ethyl-2-(2-methylpropanoylamino)butanoyl]amino]pentanoyl]amino]cyclopentane-1-carboxamide
MM-102 is a synthetic peptide compound designed as a potent and selective inhibitor of the mixed-lineage leukemia 1 (MLL1) and WD repeat-containing protein 5 (WDR5) protein-protein interaction. As a structurally optimized peptide, MM-102 is widely utilized in epigenetic research to interrogate the functional consequences of disrupting the MLL1-WDR5 axis, a key regulatory node in chromatin remodeling and gene transcription. Its well-characterized mechanism of action and specificity make it a valuable molecular probe for deciphering the role of MLL1-mediated histone methylation in diverse cellular contexts. The compound's relevance extends to studies of gene regulation, oncogenesis, and the development of chemical biology tools for targeting epigenetic modifiers.
Epigenetic modulation studies: MM-102 serves as a robust tool for investigating the molecular basis of epigenetic regulation, particularly through its ability to inhibit the interaction between MLL1 and WDR5. By preventing the assembly of the MLL1 core complex, the peptide allows researchers to dissect the downstream effects on histone H3 lysine 4 (H3K4) methylation, a critical marker of active transcription. This application is instrumental for elucidating the interplay between chromatin structure, gene expression, and cellular differentiation processes.
Protein-protein interaction analysis: The compound is frequently employed in biochemical assays and structural biology experiments to study the dynamics of MLL1-WDR5 binding. Through competitive binding assays, surface plasmon resonance, or co-immunoprecipitation approaches, MM-102 enables quantitative and qualitative assessment of the interaction interface. Insights gained from these studies inform the design of next-generation inhibitors and contribute to the broader understanding of protein complex assembly in epigenetic signaling pathways.
Chemical probe for target validation: As a selective inhibitor, MM-102 is instrumental in validating MLL1 and WDR5 as functional targets in various cellular models. Researchers utilize it to assess the biological consequences of disrupting this interaction, such as changes in transcriptional profiles or phenotypic alterations in cell lines. These experiments are crucial for establishing the causal relationships between target modulation and observed cellular outcomes, thereby supporting the development of targeted epigenetic modulators.
Peptide-based inhibitor development: MM-102's peptide structure and mechanism of action provide a template for the rational design of novel inhibitors targeting protein-protein interactions within the epigenetic machinery. Medicinal chemists and chemical biologists use it as a reference compound in structure-activity relationship studies, optimization of binding affinity, and the creation of derivatives with improved pharmacological properties for research applications. This facilitates the advancement of chemical biology strategies for modulating chromatin-associated complexes.
Transcriptional regulation research: By disrupting the MLL1-WDR5 complex, MM-102 enables detailed exploration of transcriptional control mechanisms. Researchers leverage the compound to investigate how alterations in histone methylation patterns influence the recruitment of transcriptional machinery and the activation or repression of gene expression programs. Such studies are essential for mapping the intricate regulatory networks governing cell fate, lineage commitment, and response to environmental cues, providing valuable insights into fundamental biological processes.
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