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Int. J. Mol. Sci. 2017, 18(7), 1408; doi:10.3390/ijms18071408

Identification of Direct Activator of Adenosine Monophosphate-Activated Protein Kinase (AMPK) by Structure-Based Virtual Screening and Molecular Docking Approach

Jiangsu Key Laboratory of New Drug Research and Clinical Pharmacy, School of Pharmacy, Xuzhou Medical University, Xuzhou 221004, China
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Received: 11 May 2017 / Revised: 24 June 2017 / Accepted: 27 June 2017 / Published: 30 June 2017
(This article belongs to the Special Issue Special Protein Molecules Computational Identification)
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Abstract

Adenosine monophosphate-activated protein kinase (AMPK) plays a critical role in the regulation of energy metabolism and has been targeted for drug development of therapeutic intervention in Type II diabetes and related diseases. Recently, there has been renewed interest in the development of direct β1-selective AMPK activators to treat patients with diabetic nephropathy. To investigate the details of AMPK domain structure, sequence alignment and structural comparison were used to identify the key amino acids involved in the interaction with activators and the structure difference between β1 and β2 subunits. Additionally, a series of potential β1-selective AMPK activators were identified by virtual screening using molecular docking. The retrieved hits were filtered on the basis of Lipinski’s rule of five and drug-likeness. Finally, 12 novel compounds with diverse scaffolds were obtained as potential starting points for the design of direct β1-selective AMPK activators. View Full-Text
Keywords: Adenosine 5′-monophosphate-activated protein kinase; virtual screening; molecular docking; selective activator Adenosine 5′-monophosphate-activated protein kinase; virtual screening; molecular docking; selective activator
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Huang, T.; Sun, J.; Zhou, S.; Gao, J.; Liu, Y. Identification of Direct Activator of Adenosine Monophosphate-Activated Protein Kinase (AMPK) by Structure-Based Virtual Screening and Molecular Docking Approach. Int. J. Mol. Sci. 2017, 18, 1408.

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