In organic chemistry, atoms other than carbon and hydrogen are generally referred to as heteroatoms. The most common heteroatoms are nitrogen, oxygen and sulfur. Now I present to you an article called Affinity-Based Selectivity Profiling of an In-Class Selective Competitive Inhibitor of Acyl Protein Thioesterase 2, published in 2017-02-09, which mentions a compound: 56621-48-8, mainly applied to profiling inhibitor acyl protein thioesterase; Activity-based protein profiling; chemical proteomics; inhibitor selectivity; native mass spectrometry, Category: ethers-buliding-blocks.
Activity-based protein profiling (ABPP) has revolutionized the discovery and optimization of active-site ligands across distinct enzyme families, providing a robust platform for in-class selectivity profiling. Nonetheless, this approach is less straightforward for profiling reversible inhibitors and does not access proteins outside the ABPP probe’s target profile. While the active-site competitive acyl protein thioesterase 2 (APT2) inhibitor ML349 (Ki = 120 nM) is highly selective within the serine hydrolase enzyme family, it could still interact with other cellular targets. Here we present a chemoproteomic workflow to enrich and profile candidate ML349-binding proteins. In human cell lysates, biotinylated-ML349 enriches a recurring set of proteins, including metabolite kinases and flavin-dependent oxidoreductases that are potentially enhanced by avidity-driven multimeric interactions. Confirmatory assays by native mass spectrometry and fluorescence polarization quickly rank-ordered weak off-targets, providing justification to explore ligand interactions and stoichiometry beyond ABPP.
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Reference:
Ether – Wikipedia,
Ether | (C2H5)2O – PubChem