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Chelators Targeting Matrix Metalloproteinases Library

Matrix metalloproteinases (MMPs) are a class of zinc-dependent endopeptidases that are capable of degrading almost all components of the extracellular matrix (ECM). The characteristic domain structure of MMP consists of four domains, of which the catalytic structural domain responsible for enzymatic activity contains a highly conserved zinc2+-binding region. In general, the major components of the ECM are collagens, and many other proteins that make up the basement membrane. Considering that MMPs play an important role in cancer, multiple matrix metalloproteinase inhibitors (MMPIs) have been studied by academics. Early inhibitors targeting MMP activity are designed to bind within the catalytic structural domain of these proteases. The initial therapeutic approaches are peptidomimetics, or compounds derived from the amino acid sequence of the MMP endogenous ligand.

To meet the growing demand for new structures for drug discovery projects, BOC Sciences has designed its dedicated chelators targeting matrix metalloproteinases library to generate small-molecule analogs of known ligase inhibitors with high bioactivity for the application in high-throughput screening (HTS) and high-content screening (HCS) programs.

Different biological mechanisms of intracellular localization of MMPs. Figure 1. Different biological mechanisms of intracellular localization of MMPs. (Bassiouni, W.; et al. 2021)

Library Design

  • This library of chelators that target matrix metalloproteinase based on multiple metal-binding groups can be used to screen against metalloproteinase
  • BOC Sciences’ library is able to generate a large number of high-affinity hits against several metalloprotein targets
  • Our library provides different peptidomimics or compounds derived from amino acid sequences of the MMP’s endogenous ligand that chelate catalytic zinc ions to inactivate proteases
  • In addition to the small-molecule inhibitors described above, we also offer chemically modified tetracyclines (CMTs) that can inhibit the activity of MMPs by binding to key metal ions or modulating MMP transcription

Mechanisms of regulation of intracellular MMPs activity. Figure 2. Mechanisms of regulation of intracellular MMPs activity. (Bassiouni, W.; et al. 2021)

Chelators Targeting Matrix Metalloproteinases Library Characteristics

  • No PAINS or toxic substances/unwanted functions: filtered by strict ‘Ro5-like’ physicochemical and most stringent in-house structural filters
  • All PAIN and reactive compounds are excluded from selection by internal filter applications
  • IC50, Ki, etc less than 10 μM, inhibition >25%
  • Confirmed bioactivity and safety via preclinical studies and clinical trials
  • All of the compounds have been selected by ligand efficacy and predicted binding mode
  • Structural diversity, significant efficacy, and cellular penetration
  • Structural document, IC50, and other chemical and biological data are provided
  • Tanimoto index ≥ 0.75
  • All compounds are continually updated
  • 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 Chelators Targeting Matrix Metalloproteinases Library design at competitive prices for global customers. Personalized and customized services of Chelators Targeting Matrix Metalloproteinases 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. Bassiouni, W.; et al. Multifunctional Intracellular Matrix Metalloproteinases: Implications in Disease. The FEBS Journal. 2021. 288(24): 7162-7182.
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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