TY - JOUR
T1 - In vitro screening for inhibitor of cloned Drosophila melanogaster tyramine-β-hydroxylase and docking studies
AU - Hasan, Md Nazmul
AU - Hosen, Mohammad Jakir
AU - Thakur, Prasoon Kumar
AU - Abir, Ruhshan Ahmed
AU - Zubaer, Abdullah
AU - Renkai, Guo
AU - Yoshida, Mayumi
AU - Ohta, Hiroto
AU - Lee, Jae Man
AU - Kusakabe, Takahiro
AU - Hirashima, Akinori
N1 - Funding Information:
We thank Associate Professor Chisa Aoki (Laboratory of Insect Pathology and Microbial Control, Kyushu University Graduate School) for providing the Bme21 cell line. This work was supported in part by the Program for Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN), a grant from the Ministry of Agriculture, Forestry and Fisheries of Japan (Integrated research project for plant, insect and animal using genome technology INSECT-1201) and Grant-in-Aid (no. 22248003 and 22248004 ) from the Japan Society for the Promotion of Science .
Publisher Copyright:
© 2016 Elsevier B.V.
PY - 2016/12/1
Y1 - 2016/12/1
N2 - Biogenic amines are common biologically active substances extended within the whole animal kingdom where they play vital roles as signal transducer as well as regulator of cell functions. One of these biogenic amines called octopamine (OA) is synthesized from tyramine (TA) by the catalysis of tyramine-β-hydroxylase (TβH) originated in the insect nervous system. Both TA and OA act as neurotransmitters, neurohormones and neuromodulators in the arthropod nervous system. Herein, the inhibitory activity of 1-arylimidazole-2(3H)-thiones (AITs) was tested on cloned Drosophila tyramine-β-hydroxylase (DmTβH) expressed in Bombyx mori strain. Radiolabelled 3H-TA was used to analyze the activity of AITs exhibited inhibitory effects on DmTβH, whose ID50 values range from 0.02 to 2511 nM where DmTβH was inhibited in a dose-dependent manner at pH 7.6 and 25 °C during a 30 min of incubation. To understand the catalytic role of the TβH, a three dimensional structure of the TβH from Drosophila melanogaster was constructed by homology modeling using the Phyre2 web server with 100% confidence. The modeled three-dimensional structure of TβH was used to perform the docking study with AITs. This may give more insights to precise design of inhibitors for TβH to control insect's population.
AB - Biogenic amines are common biologically active substances extended within the whole animal kingdom where they play vital roles as signal transducer as well as regulator of cell functions. One of these biogenic amines called octopamine (OA) is synthesized from tyramine (TA) by the catalysis of tyramine-β-hydroxylase (TβH) originated in the insect nervous system. Both TA and OA act as neurotransmitters, neurohormones and neuromodulators in the arthropod nervous system. Herein, the inhibitory activity of 1-arylimidazole-2(3H)-thiones (AITs) was tested on cloned Drosophila tyramine-β-hydroxylase (DmTβH) expressed in Bombyx mori strain. Radiolabelled 3H-TA was used to analyze the activity of AITs exhibited inhibitory effects on DmTβH, whose ID50 values range from 0.02 to 2511 nM where DmTβH was inhibited in a dose-dependent manner at pH 7.6 and 25 °C during a 30 min of incubation. To understand the catalytic role of the TβH, a three dimensional structure of the TβH from Drosophila melanogaster was constructed by homology modeling using the Phyre2 web server with 100% confidence. The modeled three-dimensional structure of TβH was used to perform the docking study with AITs. This may give more insights to precise design of inhibitors for TβH to control insect's population.
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U2 - 10.1016/j.ijbiomac.2016.06.026
DO - 10.1016/j.ijbiomac.2016.06.026
M3 - Article
C2 - 27355756
AN - SCOPUS:84988329686
SN - 0141-8130
VL - 93
SP - 889
EP - 895
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -