Trypsin is a serine protease whose selectivity is essential for reproducible proteolytic cleavage and protein identification based on mass spectrometry analysis. Trypsin is a serine protease from the PA clan superfamily, and is present in the digestive system of many vertebrates where it hydrolyzes proteins. Trypsin is produced in the pancreas as the inactive protease trypsin. Trypsin cleaves peptide chains mainly at the carboxyl side of amino acids lysine or arginine, except when either of them is followed by proline. It is used in many biotechnological processes which is referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized.

BOC Sciences is focused on investigating trypsin serine protease inhibitors to develop a trypsin serine protease targeted library.

Trypsin Mediated  PAR2 Stimulation Promotes Pro-migratory And Pro-invasive MVs Generation. Figure 1. Trypsin Mediated PAR2 Stimulation Promotes Pro-migratory And Pro-invasive MVs Generation. (Das, K.; et al. 2018)

Library Design

At BOC Sciences, our well-trained scientific staffs have generated a high-throughput virtual screening method based on docking approach to generate this library:

  1. A receptor-based virtual screening workflow is developed based on X-ray data for the complexes: 1J17, 1QL9, 3AAV, 3AAS, 1PPH, 1FXY
  2. The compounds in the HTS compound collection have been pre-filtered using BOC Sciences' internal filters and then docked at the active site. H-bond interaction is main spatial structure in the binding site of the complex of trypsin with lead docking molecules of potential trypsin inhibitors
  3. Finally, 1,500 potential trypsin inhibitors selected with computational chemistry and virtual screening techniques are generated successfully

Trypsin Serine Protease 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 Trypsin Serine Protease Targeted Library design at competitive prices for global customers. Personalized and customized services of Trypsin Serine Protease 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!

Reference

  1. Das, K.; et al. The Protease Activated Receptor2 Promotes Rab5a Mediated Generation of Pro-metastatic Microvesicles. Rep. 2018. 8(1):7357.
Our mission is to provide clients with a professional chemical library design platform. Empowered by high-quality services and effective research solutions, we are committed to helping customers achieve effective and successful research goals.

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Services Based on the Chemical Library Design Platform

Services Based on the Chemical Library Design Platform

BOC Sciences has rich experience in working with global customers in custom library synthesis of compounds and generating small to medium-sized libraries of target compounds. Our knowledge in generating a large number of target molecules in a remarkably shorter time enables quick biological screenings for affinities. With the target properties in mind, we deliver target molecules, by applying our extensive knowledge in drug discovery.

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