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. Issue 8 (30th June 2016)

• Record Type: Journal Article
• Authors: Shen, Yu‐Fang; Chen, Gan‐Hong; Lin, Shu‐Hsien; Lin, Gialih
• Is Part Of: Journal of the Chinese Chemical Society. Volume 63:Issue 8(2016:Aug.)
• Page Start: 709
• Page End: 715
• Publication Date: 2016-06-30
• Subjects: Lipase -- Inhibitor -- Enantioselectivity -- Carbamate -- Obesity; Chemistry -- Periodicals; Electronic journals; 540.5
• DOI: 10.1002/jccs.201600005
• Languages: English
• ISSNs: 0009-4536

Abstract

Abstract: 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. Abstract : This study provides useful information about enzyme enantioselectivity for the development of Pseudomonas species lipase inhibitors for obesity treatment.