Protein arginine N-methyltransferase 6 (PRMT6) Targeted Library

PRMT6 is a member of the protein arginine methyltransferase family, which contains 45 enzymes. PRMT6 is an important regulator responsible for RNA processing, transcriptional regulation and signal transduction. PRMT6 plays an important role in various cellular pathways, including transcriptional and cell cycle regulation, alternative splicing and DNA repair regulation, all of which have been implicated in breast cancer etiology. Therefore, PRMT6 may potentially serve as a therapeutic marker in a subset of breast cancers. In addition, PRMT6 is involved in peptidyl-arginine N-methylation and acts upstream or within multiple processes, including cellular senescence, histone H3-R2 methylation and negative regulation of nitrogen compound metabolic processes. Scientists are committed to finding specific inhibitors targeting inhibition of PRMT6 enzymatic activity that can reduce PRMT6 downstream signaling functions.

Aiming to discover PRMT6 inhibitors as antitumor agents, BOC Sciences has established a high quality protein arginine N-methyltransferase 6 (PRMT6) targeted library to carry out screening projects.

Figure 1. Protein arginine methyltransferase (PRMT) biology in skeletal muscle. (Vanlieshout, L.; Ljubicic, V. 2019)

Library Design

BOC Sciences has applied a well-designed docking-based high-throughput virtual screening approach to create this library:

1. We have developed a receptor-based virtual screening workflow based on X-ray data for the complexes with a 2-[4-(4-{(3S,4R)-4-(dimethylamino)-1-[(2-fluoro-6-methylphenyl)methyl]pyrrolidin-3-yl}phenyl)-1H-pyrazol-1-yl]acetamide derivatives using Schrödinger software
2. The binding ligands have been extracted from the PRMT6 crystal structure
3. The compounds in the HTS compound collection have been pre-filtered using BOC Sciences' internal filters and then docked at the active site: 5U6D
4. Finally, multiple potential PRMT6 inhibitors selected with computational chemistry and virtual screening techniques are generated successfully

Figure 2. Protein arginine methyltransferase (PRMT) biology in skeletal muscle. (Vanlieshout, L.; Ljubicic, V. 2019)

Protein arginine N-methyltransferase 6 (PRMT6) Targeted Library Characteristics

• No PAINS or toxic substances/unwanted functions: filtered by strict ‘Ro5-like’ physicochemical and most stringent in-house structural filters
• Bioactivity and safety confirmed by preclinical studies and clinical trials
• Structural diversity, medicinal activity, and cellular penetration
• Structural document, IC₅₀, and other chemical and biological data are provided
• All compounds are continually updated
• All of these compounds with Tanimoto index ≥ 0.85
• Compound cherry-picking service is provided

What We Deliver

• Delivered within 2 weeks in any customer-preferred format
• Powders, dry films or DMSO solutions formatted in vials, 96 or 384-well plates
• All compounds have a minimum purity of 90% assessed by ¹H NMR and HPLC
• Analytical data is provided

BOC Sciences provides professional, rapid and high-quality services of Protein arginine N-methyltransferase 6 (PRMT6) Targeted Library design at competitive prices for global customers. Personalized and customized services of Protein arginine N-methyltransferase 6 (PRMT6) Targeted Library design can satisfy any innovative scientific study demands. Our clients have direct access to our staff and prompt feedback to their inquiries. If you are interested in our services, please contact us immediately!