Comparative analysis of stimulation and binding characteristics of adenosine analogs to AMP-activated protein kinase

Abstract

To compare the stimulation and binding characteristics of adenosine analogs including AMP, IMM-H007, and M1, to AMPK, and to explore the potential mechanism underlying the regulation effect of adenosine analogs on AMPK activity, [γ-³²P]ATP assay, circular dichroism experiments and molecular docking test were performed. We found that the interactions with Thr86, Thr88, and His150 in site 1 are probably the reason why the affinities of IMM-H007, M1, and adenosine are comparable but their allosteric activation on AMPK varies greatly, partly interpreting the mechanism of AMPK activity regulated by adenosine analogs.

Keywords:

• AMP-activated protein kinase
• stimulation
• binding characteristics
• adenosine analogs
• 2′,3′,5′-tri-O-acetyl-N6-(3-hydroxylaniline) adenosine