Identification of natural allosteric inhibitor for Akt1 protein through computational approaches and in vitro evaluation

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• 作者：T. Pragna Lakshmi^a ; ^{pragnapcu@gmail.com} ; Amit Kumar^a ; ^{amit.kumar10nov@gmail.com} ; Veena Vijaykumar^b ; ^{btveenavijaykumar@gmail.com} ; Sakthivel Natarajan^b ; ^{puns2005@gmail.com} ; Ramadas Krishna^a ; ^{krishstrucbio@gmail.com}
• 关键词：PKB ; protein kinase B ; CPH ; common pharmacophore hypothesis ; RMSE ; root mean-square error ; PLS ; partial least-squares ; QSAR ; quantitative structure-activity relationship ; TCM ; traditional Chinese medicine ; HTVS ; high-throughput virtual screening ; SP ; standard precision ; XP ; extra precision ; DFT ; density functional theory ; HOMO ; higher occupied frontier orbitals ; LUMO ; lower unoccupied frontier orbitals ; MDS ; molecular dynamic simulations
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：96
• 期：Complete
• 页码：200-213
• 全文大小：4784 K
• 卷排序：96

文摘

Q7G was identified as natural allosteric inhibitor for Akt1 by performing in silico studies. It induced apoptosis, decreased p-Akt (Ser473) expression and arrested breast cancer cells in sub-G and G1 phase. Thermodynamic results provided the binding affinity of Q7G with Akt1.