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S ‐ endo ‐2‐Norbornyl‐ N ‐ n ‐butylcarbamate as a Potential Pseudomonas Lipase Inhibitor to Probe the Enantioselectivity of the Enzyme by Kinetic and Molecular Docking Evaluation
Author(s) -
Shen YuFang,
Chen GanHong,
Lin ShuHsien,
Lin Gialih
Publication year - 2016
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201600005
Subject(s) - 2 norbornyl cation , chemistry , lipase , autodock , docking (animal) , stereochemistry , pseudomonas , enzyme , biochemistry , medicine , genetics , nursing , biology , bacteria , in silico , gene
Obesity is a complex health issue and it can cause many health and social problems. Previous studies reported that lipase is a main target for obesity treatment. We synthesized R ‐ exo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamate and S ‐ exo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamate as potential pseudomonas lipase inhibitors to probe the enantioselectivity of the enzyme and demonstrated that R ‐ exo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamate had better enzyme enantioselectivity, ki and the docking model with Pseudomonas species lipase in our previous studies. In this article, we reported the property of the Pseudomonas species lipase inhibitors, R ‐and S ‐ endo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamate and compared the docking models of these two compounds with R ‐ and S ‐ exo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamates by AutoDock. We found that S ‐ endo ‐2‐norbornyl‐ N ‐ n ‐butylcarbamate has the best enantioselectivity, ki and docking model and this study could provide useful information about enzyme enantioselectivity for the development of Pseudomonas species lipase inhibitors for obesity treatment.