Galih Satrio Putra and Melanny Ika Sulistyowati and Juni Ekowati and Tutuk Budiati (2017) Pemodelan Molekul Turunan p-Metoksi sinnamoil Hidrazida Sebagai Inhibitor Checkpoint Kinase 1 dan Inhibitor Aromatase secara In silico. Pharmaceutical Science Research, 4 (2). pp. 66-80. ISSN 2407-2354

	Text (FULLTEXT) Artikel C-17.pdf Download (5MB)
	Text (PEER REVIEW) Validasi C-17.pdf Download (1MB)

Abstract

The development of anticancer drugs from ethyl p-methoxycinnamate (EPMC) derivatives continue to obtain compounds that have high ability of cancer cells apoptosis and minimal side effects. Compounds p-Methoxycinnamoyl hydrazide derivatives from EPMC structure modification were docked into the ligand-binding pocket of Check point kinase 1 enzymes (2YWP) and the aromatase enzyme (3S7S) using software Molegro Virtual Docker (MVD) Ver.5.5.We compared the Rerank score of native ligand with derived compounds p-Methoxycinnamoyl hydrazide. Rerank score of Compound 4b and 4c (-99.98 Kcal/mol and -99.80Kcal/mol) is lower than the native ligand A42 in inhibiting the enzyme checkpoint kinase 1. Rerank value of compounds p-Methoxycinnamoyl hydrazide derivatives is greater than the native ligand EXM in inhibiting the enzyme aromatase.Compounds p-Methoxycinnamoyl hydrazide derivatives especially compound 4b and 4c have anticancer mechanism by inhibiting the enzyme pathway checkpoint kinase 1 and have not activity in inhibiting the enzyme aromatase.

Actions (login required)

View Item