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ML348 是一种底物竞争性、可逆和 APT1 选择性酰基蛋白硫酯酶（APT）抑制剂（对 APT1 的 IC50/Ki = 840 nM/300 nM；对 APT2 的 IC50 & Ki >10 μM）。 ML348 可有效抑制培养物中（在 HEK293T & 小鼠 T 细胞中为 >95％；5 μM 持续 4 h）和小鼠体内（腹腔注射 50 mg/kg 后 4 小时，肺/心脏/肾脏中为 >90％，脑组织中约为 50％）的细胞 APT1 活性，而不会影响超过 15 种细胞丝氨酸水解酶和 APT2。
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WGK 3
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Alexander Adibekian et al.
Journal of the American Chemical Society, 134(25), 10345-10348 (2012-06-14)
The development of small-molecule inhibitors for perturbing enzyme function requires assays to confirm that the inhibitors interact with their enzymatic targets in vivo. Determining target engagement in vivo can be particularly challenging for poorly characterized enzymes that lack known biomarkers
Jeannie L Hernandez et al.
Cell chemical biology, 24(1), 87-97 (2017-01-10)
The multidomain scaffolding protein Scribble (Scrib) organizes key signaling complexes to specify basolateral cell polarity and suppress aberrant growth. In many human cancers, genetically normal Scrib mislocalizes from cell-cell junctions to the cytosol, correlating with enhanced growth signaling and malignancy.
Rahul S Kathayat et al.
Nature chemical biology, 13(2), 150-152 (2016-12-20)
Hundreds of human proteins are modified by reversible palmitoylation of cysteine residues (S-palmitoylation), but the regulation of depalmitoylation is poorly understood. Here, we develop 'depalmitoylation probes' (DPPs), small-molecule fluorophores, to monitor the endogenous activity levels of 'erasers' of S-palmitoylation, acylprotein
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