MLCK inhibitor peptide 18

Product Name:MLCK inhibitor peptide 18

CAS No:224579-74-2

Purity:95%

Molar Mass:1324.6

Chemical Formula:C60H105N23O11

Storage:Store at -20 degrees Celsius

Sequence:RKKYKYRRK

Target:myosin light chain kinase (MLCK)

Application:MLCK Inhibitor Peptide 18 is a synthetic peptide specifically designed to inhibit myosin light chain kinase (MLCK), an enzyme crucial for regulating muscle contraction and cytoskeletal dynamics. This peptide blocks the phosphorylation of myosin light chains, thereby preventing the downstream effects of MLCK activation. MLCK Inhibitor Peptide 18 is an essential tool for research focused on understanding the role of MLCK in smooth muscle contraction, cell motility, and various physiological processes. With its high specificity and purity, this inhibitor peptide ensures consistent and reliable results, making it invaluable for studies in muscle physiology and cell biology.

Current Research:

MLCK inhibitor peptide 18 is a synthetic, cell-permeable nonapeptide that selectively inhibits myosin light chain kinase (MLCK), an enzyme pivotal in modulating smooth muscle contraction and various cellular motility processes. This peptide exhibits an IC?? of 50 nM for MLCK, demonstrating high specificity by showing 4,000-fold less potency against Ca2?/calmodulin-dependent protein kinase II (CaMKII) and negligible inhibition of protein kinase A (PKA).
Mechanism of Action
MLCK inhibitor peptide 18 operates as a competitive inhibitor concerning the peptide substrate, with a K? of 52 nM, and displays mixed-mode inhibition relative to ATP. It does not interfere with the activation of MLCK by calmodulin, ensuring targeted inhibition of MLCK activity without affecting upstream regulatory mechanisms.
Research Applications
Due to its high specificity and cell permeability, MLCK inhibitor peptide 18 is extensively utilized in research to dissect the role of MLCK in various physiological and pathological contexts. It has been instrumental in studies focusing on smooth muscle function, cell motility, and the integrity of the actin cytoskeleton. For instance, it has been employed to restore barrier function in in vitro models of intestinal disease by inhibiting MLCK-mediated phosphorylation of myosin light chains, thereby elucidating the enzyme's role in epithelial permeability.
Considerations
When utilizing MLCK inhibitor peptide 18 in experimental settings, it is crucial to account for its concentration-dependent effects and ensure specificity by including appropriate controls. Given its competitive inhibition mechanism, varying substrate concentrations can influence its efficacy, necessitating careful optimization of experimental conditions.
Conclusion
MLCK inhibitor peptide 18 serves as a potent and selective tool for investigating MLCK's functions in cellular processes. Its application has significantly advanced the understanding of MLCK-mediated pathways, contributing to insights into muscle contraction, cell motility, and barrier function regulation.

Reference:

Marchenko, A. V., Stepanova, E. O., Sekridova, A. V., Sidorova, M. V., Bushuev, V. N., Bespalova, Z. D., & Shirinsky, V. P. (2010). Novel peptide inhibitors of myosin light chain kinase suppress the hyperpermeability of vascular endothelium.?Biophysics,?55, 926-930.