WL 47 – dimer

Product Name:WL 47 - dimer

Purity:95%

Molar Mass:1844.3

Chemical Formula:C80H130N24O18S4

Storage:Store at -20 degrees Celsius

Sequence:CSWMRLK CSWMRLK

Target:CAV1

Application:

WL 47-dimer is associated with Caveolin-1 (CAV1), a scaffolding protein involved in the formation of caveolae, small invaginations in the plasma membrane that regulate signal transduction, lipid metabolism, and endocytosis. CAV1 plays a critical role in various cellular processes, including cell signaling, cholesterol homeostasis, and tumor suppression. WL 47-dimer's interaction with CAV1 suggests it could be used in research to explore CAV1's role in cellular pathways, such as its influence on membrane dynamics, cancer progression, or cardiovascular diseases. This makes WL 47-dimer valuable in studies aimed at understanding the molecular mechanisms governed by CAV1.

Current Research:

WL 47 dimer is a synthetic peptide that functions as a high-affinity ligand for caveolin-1 (CAV-1), a scaffolding protein involved in the formation of caveolae—small invaginations in the plasma membrane. By simultaneously occupying two binding sites on CAV-1, WL 47 dimer induces the dissociation of CAV-1 oligomers, thereby modulating caveolae dynamics and associated cellular processes.

Structural Composition

WL 47 dimer consists of two peptide chains, each with the sequence Cys-Ser-Trp-Met-Arg-Leu-Lys (CSWMRLK). These chains are linked via a disulfide bridge between the cysteine residues at the N-terminus of each chain, forming a dimeric structure. This design enables the peptide to engage two CAV-1 binding sites simultaneously, enhancing its efficacy in disrupting CAV-1 oligomers.

Mechanism of Action

By binding to CAV-1 with a dissociation constant (K_d) of 23 nM, WL 47 dimer effectively disrupts CAV-1 oligomers. This disruption can influence various cellular functions, including endocytosis, signal transduction, and lipid metabolism, all of which are associated with caveolae. Notably, WL 47 dimer exhibits high selectivity for CAV-1 over other proteins such as bovine serum albumin (BSA), casein, and hen egg white lysozyme (HEWL), underscoring its specificity in targeting CAV-1-mediated pathways.

Research Applications

WL 47 dimer serves as a valuable tool in biomedical research for:

Investigating CAV-1 Function: By inducing the dissociation of CAV-1 oligomers, researchers can study the role of CAV-1 in cellular processes and its involvement in various diseases.

Exploring Caveolae Dynamics: Understanding how the disruption of CAV-1 oligomers affects caveolae formation and function can provide insights into membrane biology and related pathologies.

Developing Therapeutic Strategies: Targeting CAV-1 oligomerization has potential therapeutic implications in conditions where caveolae and CAV-1 play critical roles, such as cardiovascular diseases and cancer.

Conclusion

WL 47 dimer is a potent and selective ligand for caveolin-1, capable of disrupting its oligomeric structures. Its application in research enhances the understanding of CAV-1's role in cellular physiology and offers potential avenues for therapeutic intervention in diseases associated with caveolae dysfunction.

Reference:

Gilliam, A. J., Smith, J. N., Flather, D., Johnston, K. M., Gansmiller, A. M., Fishman, D. A., ... & Weiss, G. A. (2016). Affinity-guided design of caveolin-1 ligands for deoligomerization. Journal of medicinal chemistry, 59(8), 4019-4025.