Abstract
A series of α,α′-bis(2-oxo-3,3,3-trifluoropropylthio)alkanes was synthesized by the alkylation of the appropriate α,α′-alkanedithiol with 3-bromo-1,1,1-trifluoropropan-2-one. The compounds were tested for in vitro inhibition of insect juvenile hormone esterase (JHE), electric eel acetylcholinesterase (AChE), porcine carboxylesterase, and yeast lipase. Inhibition of hemolymph JHE from fifth instar larvae of the cabbage looper, Trichoplusia ni (Hübner) (Lepidotera: Noctuidae), was in the nanomolar range for many compounds. The inhibition of the other three enzymes was only moderate in comparison to JHE. The inhibition of JHE was compared to carbon chain length, differing heteroatoms, and presence of methyl side-chains. The most effective compound was 1,1,1,16,16,16-hexafluoro-4,13-dithiahexadecane-2,15-dione (I50: 8.2 × 10-10 M). The kinetics of inhibition were found to be time-dependent against both JHE and AChE enzymes using representative compounds of both high and low inhibitory potential. Second-order inhibition velocity constants were determined and found to be in agreement with the I50 values.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 112-124 |
| Number of pages | 13 |
| Journal | Pesticide Biochemistry and Physiology |
| Volume | 33 |
| Issue number | 2 |
| DOIs | |
| State | Published - 1989 |
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ASJC Scopus subject areas
- Agronomy and Crop Science
- Biochemistry
- Physiology
Cite this
New trifluoropropanone sulfides as highly active and selective inhibitors of insect juvenile hormone esterase. / Székács, András; Hammock, Bruce D.; Abdel-Aal, Yehia A I; Halarnkar, Premjit P.; Philpott, Matthew; Matolcsy, György.
In: Pesticide Biochemistry and Physiology, Vol. 33, No. 2, 1989, p. 112-124.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - New trifluoropropanone sulfides as highly active and selective inhibitors of insect juvenile hormone esterase
AU - Székács, András
AU - Hammock, Bruce D.
AU - Abdel-Aal, Yehia A I
AU - Halarnkar, Premjit P.
AU - Philpott, Matthew
AU - Matolcsy, György
PY - 1989
Y1 - 1989
N2 - A series of α,α′-bis(2-oxo-3,3,3-trifluoropropylthio)alkanes was synthesized by the alkylation of the appropriate α,α′-alkanedithiol with 3-bromo-1,1,1-trifluoropropan-2-one. The compounds were tested for in vitro inhibition of insect juvenile hormone esterase (JHE), electric eel acetylcholinesterase (AChE), porcine carboxylesterase, and yeast lipase. Inhibition of hemolymph JHE from fifth instar larvae of the cabbage looper, Trichoplusia ni (Hübner) (Lepidotera: Noctuidae), was in the nanomolar range for many compounds. The inhibition of the other three enzymes was only moderate in comparison to JHE. The inhibition of JHE was compared to carbon chain length, differing heteroatoms, and presence of methyl side-chains. The most effective compound was 1,1,1,16,16,16-hexafluoro-4,13-dithiahexadecane-2,15-dione (I50: 8.2 × 10-10 M). The kinetics of inhibition were found to be time-dependent against both JHE and AChE enzymes using representative compounds of both high and low inhibitory potential. Second-order inhibition velocity constants were determined and found to be in agreement with the I50 values.
AB - A series of α,α′-bis(2-oxo-3,3,3-trifluoropropylthio)alkanes was synthesized by the alkylation of the appropriate α,α′-alkanedithiol with 3-bromo-1,1,1-trifluoropropan-2-one. The compounds were tested for in vitro inhibition of insect juvenile hormone esterase (JHE), electric eel acetylcholinesterase (AChE), porcine carboxylesterase, and yeast lipase. Inhibition of hemolymph JHE from fifth instar larvae of the cabbage looper, Trichoplusia ni (Hübner) (Lepidotera: Noctuidae), was in the nanomolar range for many compounds. The inhibition of the other three enzymes was only moderate in comparison to JHE. The inhibition of JHE was compared to carbon chain length, differing heteroatoms, and presence of methyl side-chains. The most effective compound was 1,1,1,16,16,16-hexafluoro-4,13-dithiahexadecane-2,15-dione (I50: 8.2 × 10-10 M). The kinetics of inhibition were found to be time-dependent against both JHE and AChE enzymes using representative compounds of both high and low inhibitory potential. Second-order inhibition velocity constants were determined and found to be in agreement with the I50 values.
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U2 - 10.1016/0048-3575(89)90002-3
DO - 10.1016/0048-3575(89)90002-3
M3 - Article
VL - 33
SP - 112
EP - 124
JO - Pesticide Biochemistry and Physiology
JF - Pesticide Biochemistry and Physiology
SN - 0048-3575
IS - 2
ER -