Dextran sulfate sodium salt (MW 35000-45000)

Targeted protein degradation(TPD) is a novel and promising approach to new drug discovery and development. It shows great potential for treating diseases with “undruggable” pathogenic protein targets and for overcoming drug resistance. Molecular glues and PROTACs are both targeted protein degraders that have attracted the most attention.

Molecular glues are small molecular degraders that mainly induce novel interaction between an E3 ligase and a target protein to form a ternary complex, leading to protein ubiquitination and subsequent proteasome degradation. Compared with PROTACs, molecular glues generally possess more favorable drug-like properties, such as lower MW, higher cell permeability, and better oral absorption. Molecular glues are emerging as a promising new therapeutic strategy.

MCE supplies a unique collection of 39 molecular glues which target various proteins. MCE Molecular Glue Compound Library is a useful tool to conduct scientific research and disease mechanism study.

Covalent inhibitors are small molecules that can bind specifically to target proteins through covalent bonds and inhibit their biological functions. Although for a long time, covalent targeting has been playing a subordinate role in drug discovery, with an increasing number of reports on successful clinical applications of such drugs, the potential of these agents is now being acknowledged. Currently, cysteine is the most common covalent amino acid residue in a variety of covalent drugs, and various warheads have been developed that can react with cysteine, providing the key building blocks for covalent drugs to form covalent bonds.

To meet the development needs of covalent inhibitors targeting cysteine, MCE has designed a unique collection of 3,165 fragments with different covalent warheads that target cysteine. The MCE Cysteine Targeted Covalent Fragment Library is designed using the following covalent warheads: Acrylamides, Propiolic acid ester, Dimethylamine functionalized acrylamides, Chloroacetamides, Acrylonitrile, 2-Cyanoacrylamide, Aziridine, Haloacetamide, etc. All fragments are pre-filtered with the Rule of Three restrictions which can be used for fragment-based covalent drug development.

Covalent inhibitors are small molecules that can bind specifically to target proteins through covalent bonds and inhibit their biological functions. Although for a long time, covalent targeting has been playing a subordinate role in drug discovery, with an increasing number of reports on successful clinical applications of such drugs, the potential of these agents is now being acknowledged. Currently, cysteine is the most common covalent amino acid residue in a variety of covalent drugs, and various warheads have been developed that can react with cysteine, providing the key building blocks for covalent drugs to form covalent bonds.

To meet the development needs of covalent inhibitors targeting cysteine, MCE has designed a unique collection of 4,528 compounds with different covalent warheads that target cysteine. The MCE Cysteine Targeted Covalent Library is designed using the following covalent warheads: Acrylamides, Propiolic acid ester, Dimethylamine functionalized acrylamides, Chloroacetamides, Acrylonitrile, 2-Cyanoacrylamide, Aziridine, Haloacetamide, etc.

19F-NMR has proved to be a detection mode in fragment-based drug discovery (FBDD) for studies of protein structure and interactions. 19F shows high sensitivity for NMR detection, and the exquisite sensitivity of 19F chemical shifts and linewidths to ligand binding all make it a valuable approach in FBDD.F (Fluorine) -Fragments can be used for 19F-NMR detection after binding to target proteins, and can be used as an effective 19F-NMR tool for FBDD.

MCE designs a unique collection of 4,971 F-fragments, all of which obey a heuristic rule called the “Rule of Three (RO3)”, in which molecular weight ≤300 Da, the number of hydrogen bond donors (H-donors) ≤3, the number of hydrogen bond acceptors (H-acceptors) is ≤3 and cLogP is ≤3. This F-fragments library is an important source of lead-like drugs.

Fragment-based drug discovery (FBDD) is well suited for discovering both drug leads and chemical probes of protein function; it can cover broad swaths of chemical space and allows the use of creative chemistry. Fragment-based drug discovery is well-established in industry and has resulted in a variety of drugs entering clinical trials, with two, vemurafenib and venetoclax, already approved. FBDD also has key attractions for academia. Notably, it is able to tackle difficult or novel targets for which no chemical matter may be found in existing HTS collections.

MCE designs a unique collection of 22,464 fragment compounds, all of which obey a heuristic rule called the “Rule of Three (RO3) ”, in which molecular weight ≤300 Da, the number of hydrogen bond donors (H-donors) ≤3, the number of hydrogen bond acceptors (H-acceptors) is ≤3 and cLogP is ≤3. This library is an important source of lead-like drugs.

Natural products are an attractive source with varied structures that exhibit potent biological activities, and desirable pharmacological profiles. The core scaffold of a natural product can also provide a biologically validated framework upon which to display diverse functional groups. Inspired by bioactive natural products, natural product-like compounds, occupying the same chemical space, are ideally suited to explore and to facilitate understanding of biological pathways.

MCE 10K Natural Product-like Compound Library consists of 10,000 natural product-like compounds. Each compound has scaffold of natural products or Tanimoto coefficient >0.6 with natural products. The natural-likeness scoring of these compounds is >-2. What’s more, compounds in the library are drug-like and readily available for re-supply, making it a powerful tool for new drug research and development. It can be widely applied in high-throughput screening (HTS) and high-content screening (HCS).

MCE Kanamycin sulfate (100x), Sterile is an aminoglycoside antibiotic purified from Streptomyces kanamyceticus. It acts by binding to the 30S subunit of the bacterial ribosome and inhibiting protein synthesis in susceptible bacteria.