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- W4384561207 abstract "Cancer is a major public health concern requiring novel treatment approaches. Enzyme-instructed self-assembly (EISA) provides a unique approach for selectively inhibiting cancer cells. However, the structure and activity correlation of EISA remains to be explored. This study investigates new EISA substrates of alkaline phosphatase (ALP) to hinder ovarian cancer cells. Analogues 2-8 were synthesized by modifying the amino acid residues of a potent EISA substrate 1 that effectively inhibits the growth of OVSAHO, a high-grade serous ovarian cancer (HGSOC) cell line. The efficacy of 2-8 against OVSAHO was assessed, along with the combination of substrate 1 with clinically used drugs. The results reveal that substrate 1 displays the highest cytotoxicity against OVSAHO cells, with an IC50 of around 8 μM. However, there was limited synergism observed between substrate 1 and the tested clinically used drugs. These findings indicate that EISA likely operates through a distinct mechanism that necessitates further elucidation." @default.
- W4384561207 created "2023-07-18" @default.
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- W4384561207 date "2023-07-17" @default.
- W4384561207 modified "2023-10-16" @default.
- W4384561207 title "Evaluating Alkaline Phosphatase-Instructed Self-Assembly of <scp>d</scp>-Peptides for Selectively Inhibiting Ovarian Cancer Cells" @default.
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- W4384561207 doi "https://doi.org/10.1021/acs.jmedchem.3c00949" @default.
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