IMR Press / FBL / Volume 13 / Issue 8 / DOI: 10.2741/2891

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article

Electrochemical impedance spectroscopy for the study of juvenile hormones – recombinant protein interactions

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1 Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Tuwima 10, 10-747 Olsztyn, Poland
2 Institute of Molecular Biology and Genetics, Ukrainian National Academy of Sciences, Zabolotnogo 150, 03-143 Kyiv, Ukraine
3 Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland

*Author to whom correspondence should be addressed.

 

Front. Biosci. (Landmark Ed) 2008, 13(8), 2866–2874; https://doi.org/10.2741/2891
Published: 1 January 2008
Abstract

The interactions of recombinant juvenile hormone binding protein (His8-rJHBP) with juvenile hormones (JHs), methoprene and farnesol have been studied with electrochemical impedance spectroscopy (EIS). The protein was immobilized on the dodecanethiol (DDT) modified gold electrodes. Each step of electrode modification has been confirmed with cyclic voltammetry (CV) and electrochemical impedance spectroscopy (EIS). The conformation changes of His8-rJHBP upon JHs and methoprene binding have been presented. The EIS determined association constants in the JHs analogs – immobilized His8-rJHBP system indicate that lack of the epoxide moiety in methoprene molecule is not critical for observed high affinity of this compound to the binding region of the His8-rJHBP protein.

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