Flavonoids activating adenosine monophosphate-activated protein kinase

• Published in: Applied biological chemistry Vol. 58; no. 1; pp. 13 - 19
• Main Authors: Yong, Y., Konkuk University, Seoul, Republic of Korea, Shin, S.Y., Konkuk University, Seoul, Republic of Korea, Jung, Y., Konkuk University, Seoul, Republic of Korea, Jung, H., Konkuk University, Seoul, Republic of Korea, Ahn, S., Konkuk University, Seoul, Republic of Korea, Chong, Y., Konkuk University, Seoul, Republic of Korea, Lim, Y., Konkuk University, Seoul, Republic of Korea
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Netherlands 01.02.2015; Springer Nature B.V; 한국응용생명화학회
• Subjects: Adenosine; Adenosine kinase; Adenosine monophosphate; AMP; AMP-activated protein kinase; AMPK,Kinase assay,Kaempferide,In silico docking; Applied Microbiology; Binding sites; Biological Techniques; Bioorganic Chemistry; Chemistry; Chemistry and Materials Science; Crystal structure; Crystallography; Docking; FLAVONOIDE; FLAVONOIDES; FLAVONOIDS; Kinases; molecular models; Phosphates; Phosphorylation; Protein kinase; Proteins; Substrates; Western blotting; 농학; Kaempferide; AMPK; In silico docking; Kinase assay; Flavonoid
• ISSN: 1738-2203; 2468-0834; 2234-344X; 2468-0842
• DOI: 10.1007/s13765-015-0003-4

Eighteen flavonoids were tested as adenosine monophosphate-activated protein kinase (AMPK) activators. The AMPK activation induced by kaempferide was 1.75 times better than the value obtained at 100 % AMPK phosphorylation. Western blotting analysis of kaempferide demonstrated that it increased the phosphorylation of AMPK in vitro. In silico docking results carried out to elucidate the binding mode between kaempferide and AMPK showed the docking pose of kaempferide in the binding site of AMPK was similar to that of the substrate contained in the crystallographic structure of AMPK. Flavonoids, including kaempferide, are promising potential AMPK activators.