MM-401 TFA is a peptide-derived inhibitor scaffold widely used to probe histone methyltransferase recognition and chromatin-associated interactions. Its sequence mimics key lysine-containing motifs within histone tails. Researchers investigate binding thermodynamics, structural rearrangements, and epigenetic complex formation. Applications span chromatin biochemistry, probe development, and structure-activity relationship analysis.
CAT No: R2692
CAS No:1442106-11-7
Synonyms/Alias:MM-401 TFA;1442106-11-7;MM-401 (TFA);CHEMBL4099772;HY-19554A;DA-65550;CS-0104334;F82461;N-[(3R,6S,9S,12R)-9-[3-(diaminomethylideneamino)propyl]-6-ethyl-12-methyl-2,5,8,11-tetraoxo-3-phenyl-1,4,7,10-tetrazacyclohexadec-12-yl]-2-methylpropanamide;2,2,2-trifluoroacetic acid;
MM-401 Tfa is a synthetic peptide compound designed as a potent and selective inhibitor of the mixed-lineage leukemia 1 (MLL1) histone methyltransferase complex. As an engineered peptide, it specifically targets the interaction between MLL1 and WDR5, a scaffolding protein essential for the assembly and activity of the MLL1 complex. Through its unique sequence and structural features, MM-401 Tfa disrupts critical protein-protein interactions involved in epigenetic regulation, making it an invaluable tool for investigating chromatin remodeling, transcriptional control, and the functional consequences of MLL1-mediated histone modifications. Its biochemical properties and targeted mechanism of action have positioned it as a key reagent for advanced studies in epigenetics, gene expression, and peptide-based inhibitor development.
Epigenetic research: MM-401 Tfa serves as a highly specific probe for dissecting the role of MLL1 in histone H3 lysine 4 (H3K4) methylation, a modification closely associated with active gene transcription. By selectively inhibiting the MLL1-WDR5 interaction, the peptide enables researchers to interrogate the mechanistic basis of chromatin state transitions and the recruitment of transcriptional machinery to gene promoters. Its use facilitates detailed studies on how MLL1-dependent methylation patterns influence gene activation and cellular identity, providing valuable insights into the broader field of epigenetic regulation.
Protein-protein interaction studies: The ability of MM-401 Tfa to disrupt a defined protein-protein interface makes it an exemplary tool for validating the functional significance of the MLL1-WDR5 complex. Researchers can employ the peptide in biochemical assays, co-immunoprecipitation experiments, and structural analyses to map interaction domains, assess binding affinities, and characterize the consequences of complex disruption. Such studies are essential for understanding the modular assembly of chromatin-modifying complexes and for identifying potential intervention points in epigenetic signaling pathways.
Peptide inhibitor development: As a rationally designed peptide antagonist, MM-401 Tfa provides a template for the development of next-generation peptide-based inhibitors targeting chromatin-associated proteins. Its sequence and mode of action offer a model for structure-activity relationship (SAR) studies, enabling medicinal chemists and peptide engineers to optimize selectivity, cellular uptake, and stability. The compound's use in screening and optimization workflows supports the advancement of novel research tools for modulating epigenetic processes.
Gene expression analysis: By modulating the activity of the MLL1 complex, MM-401 Tfa allows researchers to examine downstream effects on gene expression profiles in various cell types. Its application in transcriptomics, reporter assays, and chromatin immunoprecipitation (ChIP) experiments provides a direct means to link MLL1-dependent histone methylation to specific transcriptional outcomes. Such analyses are critical for elucidating the regulatory networks governing cell differentiation, proliferation, and lineage commitment.
Functional genomics: The targeted inhibition enabled by MM-401 Tfa supports functional genomics investigations aimed at decoding the role of MLL1 in development, stem cell biology, and disease models. By integrating the peptide into loss-of-function studies, researchers can systematically probe the genetic dependencies and epigenetic landscapes shaped by MLL1 activity. This approach aids in identifying key regulatory nodes and in characterizing the phenotypic consequences of perturbing chromatin-modifying complexes at the molecular level.
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5. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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