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Nguyen Phuong Thao,Bui Thi Thuy Luyen,Nguyen Thi Thanh Ngan,Le Duc Dat,Nguyen Xuan Cuong,Nguyen Hoai Nam,Phan Van Kiem,Seok Bean Song,Chau Van Minh,김영호 대한약학회 2015 Archives of Pharmacal Research Vol.38 No.5
Peroxisome proliferator-activated receptors(PPARs) are ligand-activated transcription factors thatregulate the expression of multiple genes involved inmetabolic, anti-inflammatory, and developmental processes. This study evaluated the PPARs transactivationaleffects of thirteen cembranoid diterpenoids 1–13 from thesoft coral Lobophytum crassum, using PPAR-responsiveelements–luciferase reporter and GAL4–PPAR chimeraassays. All isolated compounds activated the transcriptionof PPARs in a dose-dependent manner, with EC50 valuesranging from 2.07 ± 1.73 to 130.20 ± 1.85 lM. Moreover,compounds 6–9 affected the transactivation of allthree PPAR types, PPARa, c, b(d), in a dose-dependentmanner, with EC50 values in a ranging from 11.92 ± 1.23to 122.50 ± 2.12 lM. These results provide a scientificrationale for further studies on the soft coral L. crassum andits diterpenoid constituents to develop medicinal productsagainst inflammatory and metabolic diseases.
The effective model of the human Acetyl-CoA Carboxylase inhibition by aromatic-structure inhibitors
Nguyen Truong Cong Minh,Bui Tho Thanh,Le Xuan Truong,Nguyen Thi Bang Suong,Le Thi Xuan Thao 한국전기전자학회 2017 전기전자학회논문지 Vol.21 No.3
The research investigates the inhibition of fatty acid biosynthesis of the human Acetyl-CoA Carboxylase enzyme by the aromatic-structure inhibitors (also known as ligands) containing variables of substituents, contributing an important role in the treatment of fatty-acid metabolic syndrome expressed by the group of cardiovascular risk factors increasing the incidence of coronary heart disease and type-2 diabetes. The effective interoperability between ligand and enzyme is characterized by a 50% concentration of enzyme inhibitor (IC50) which was determined by experiment, and the factor of geometry structure of the ligands which are modeled by quantum mechanical methods using HyperChem 8.0.10 and Gaussian 09W softwares, combining with the calculation of quantum chemical and chemico-physical structural parameters using HyperChem 8.0.10 and Padel Descriptor 2.21 softwares. The result data are processed with the combination of classical statistical methods and modern bioinformatics methods using the statistical softwares of Department of Pharmaceutical Technology – Jadavpur University – India and R v3.3.1 software in order to accomplish a model of the quantitative structure - activity relationship between aromatic-structure ligands inhibiting fatty acid biosynthesis of the human Acetyl-CoA Carboxylase.
The effective model of the human Acetyl-CoA Carboxylase inhibition by aromatic-structure inhibitors
Minh, Nguyen Truong Cong,Thanh, Bui Tho,Truong, Le Xuan,Suong, Nguyen Thi Bang,Thao, Le Thi Xuan Institute of Korean Electrical and Electronics Eng 2017 전기전자학회논문지 Vol.21 No.3
The research investigates the inhibition of fatty acid biosynthesis of the human Acetyl-CoA Carboxylase enzyme by the aromatic-structure inhibitors (also known as ligands) containing variables of substituents, contributing an important role in the treatment of fatty-acid metabolic syndrome expressed by the group of cardiovascular risk factors increasing the incidence of coronary heart disease and type-2 diabetes. The effective interoperability between ligand and enzyme is characterized by a 50% concentration of enzyme inhibitor ($IC_{50}$) which was determined by experiment, and the factor of geometry structure of the ligands which are modeled by quantum mechanical methods using HyperChem 8.0.10 and Gaussian 09W softwares, combining with the calculation of quantum chemical and chemico-physical structural parameters using HyperChem 8.0.10 and Padel Descriptor 2.21 softwares. The result data are processed with the combination of classical statistical methods and modern bioinformatics methods using the statistical softwares of Department of Pharmaceutical Technology - Jadavpur University - India and R v3.3.1 software in order to accomplish a model of the quantitative structure - activity relationship between aromatic-structure ligands inhibiting fatty acid biosynthesis of the human Acetyl-CoA Carboxylase.