| Literature DB >> 32328963 |
M J Fragoso-Vázquez1,2, D Méndez-Luna2, M C Rosales-Hernández3, G R Luna-Palencia2, A Estrada-Pérez2, Benedicte Fromager4, I Vásquez-Moctezuma5, J Correa-Basurto6.
Abstract
Glutaminase plays an important role in carcinogenesis and cancer cell growth. This biological target is interesting against cancer cells. Therefore, in this work, in silico [docking and molecular dynamics (MD) simulations] and in vitro methods (antiproliferative and LC-MS metabolomics) were employed to assay a hybrid compound derived from glutamine and valproic acid (Gln-VPA), which was compared with 6-diazo-5-oxo-L-norleucine (DON, a glutaminase inhibitor) and VPA (contained in Gln-VPA structure). Docking results from some snapshots retrieved from MD simulations show that glutaminase recognized Gln-VPA and DON. Additionally, Gln-VPA showed antiproliferative effects in HeLa cells and inhibited glutaminase activity. Finally, the LC-MS-based metabolomics studies on HeLa cells treated with either Gln-VPA (IC60 = 8 mM) or DON (IC50 = 3.5 mM) show different metabolomics behaviors, suggesting that they modulate different biological targets of the cell death mechanism. In conclusion, Gln-VPA is capable of interfering with more than one pharmacological target of cancer, making it an interesting drug that can be used to avoid multitherapy of classic anticancer drugs.Entities:
Keywords: Anti-proliferative LC–MS-based metabolomic; Dual-target inhibitor; Gln-VPA; Glutaminase
Year: 2020 PMID: 32328963 DOI: 10.1007/s11030-020-10089-z
Source DB: PubMed Journal: Mol Divers ISSN: 1381-1991 Impact factor: 2.943