Acts as inhibitor of neural Wiskott-Aldrich syndrome protein (N-WASP) by stabilizing the autoinhibited state of the protein. It inhibits actin assembly stimulated by phosphatidylinositol 4,5-bisphosphate (pip2), but does not directly inhibit actin
CAT No: R0915
CAS No:380488-27-7
Synonyms/Alias:187-1, N-WASP inhibitor;380488-27-7;CHEMBL436918;Cyclo(L-glutaminyl-L-lysyl-D-phenylalanyl-D-prolyl-D-phenylalanyl-L-phenylalanyl-D-prolyl-L-glutaminyl-L-lysyl-D-phenylalanyl-D-prolyl-D-phenylalanyl-L-phenylalanyl-D-prolyl);3-[(3S,6R,9R,15R,18S,21S,24R,30S,33R,36R,42R,45S,48S,51R)-18,45-bis(4-aminobutyl)-48-(3-amino-3-oxopropyl)-3,6,15,30,33,42-hexabenzyl-2,5,8,14,17,20,23,29,32,35,41,44,47,50-tetradecaoxo-1,4,7,13,16,19,22,28,31,34,40,43,46,49-tetradecazapentacyclo[49.3.0.09,13.024,28.036,40]tetrapentacontan-21-yl]propanamide;QKFPFFPQKFPFFP;BDBM50175058;AKOS024456924;PD079245;G13303;cyclo[L-Lys-D-Phe-D-Pro-D-Phe-L-Phe-D-Pro-L-Gln]2;S-380488-27-7;
187-1, N-WASP inhibitor, is a small molecule compound designed to selectively target the neural Wiskott-Aldrich syndrome protein (N-WASP), a key regulator of actin cytoskeleton dynamics. As an allosteric modulator, it interferes with the activation of N-WASP, thereby impeding downstream signaling pathways that control actin polymerization and cellular motility. This inhibitor holds particular significance in cellular and molecular biology research, as N-WASP is integral to processes such as endocytosis, cell migration, and membrane trafficking. The ability to modulate N-WASP function with high specificity makes 187-1 a valuable tool for dissecting the roles of actin-associated proteins in various physiological and pathological contexts.
Cytoskeletal Dynamics Research: In studies focused on the mechanisms of cytoskeletal remodeling, 187-1 provides a targeted approach to dissecting the role of N-WASP in actin filament assembly. By inhibiting N-WASP-mediated activation of the Arp2/3 complex, researchers can delineate the contribution of this pathway to lamellipodia and filopodia formation, cell shape regulation, and motility. The compound enables precise perturbation of actin nucleation events, offering critical insights into the spatial and temporal control of cytoskeletal architecture.
Cell Migration and Invasion Assays: The inhibitor is widely employed in experimental models investigating cell motility, including wound healing, transwell migration, and invasion assays. By specifically blocking N-WASP-driven actin polymerization, 187-1 allows researchers to evaluate the dependence of migratory and invasive behaviors on this pathway. Such studies are essential for unraveling the molecular underpinnings of processes such as cancer metastasis, neuronal pathfinding, and immune cell trafficking, where cell movement is tightly regulated by actin dynamics.
Endocytosis and Membrane Trafficking Studies: N-WASP plays a pivotal role in clathrin-mediated endocytosis and vesicular trafficking by facilitating actin assembly at sites of membrane remodeling. Application of 187-1 in these contexts enables the selective inhibition of N-WASP-dependent endocytic events, allowing for the dissection of distinct molecular steps involved in vesicle formation, cargo uptake, and intracellular transport. This approach is particularly valuable for distinguishing the contributions of N-WASP from other actin-regulatory proteins in membrane trafficking pathways.
Signal Transduction Pathway Analysis: Investigators studying the integration of extracellular signals with cytoskeletal responses utilize 187-1 to probe the involvement of N-WASP in transducing upstream cues into actin reorganization. By modulating N-WASP activity, it becomes possible to map signaling cascades that converge on actin assembly, such as those mediated by Rho GTPases, phosphoinositides, or tyrosine kinases. This application supports the elucidation of how specific signaling networks orchestrate cytoskeletal responses to environmental stimuli.
Drug Discovery and Target Validation: As a selective chemical probe, 187-1 is instrumental in validating N-WASP as a potential target for therapeutic intervention in diseases characterized by aberrant actin dynamics. Its use in high-content screening and functional genomics platforms enables the identification of phenotypic changes upon N-WASP inhibition, facilitating the assessment of on-target effects and off-target liabilities. Such studies contribute to the early-stage evaluation of actin-regulatory pathways as druggable nodes in a range of research models, from oncology to neurobiology.
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