A hypothesis to account for the selective and diverse actions of neonicotinoid insecticides at their molecular targets,nicotinic acetylcholine receptors: catch and release in hydrogen bond networks |
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Authors: | Makoto Ihara Masaru Shimomura Chiharu Ishida Hisashi Nishiwaki Miki Akamatsu David B Sattelle Kazuhiko Matsuda |
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Institution: | (1) RIKEN Harima Institute, SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo, Hyogo 679-5148, Japan;(2) Invertebrate Gene Function Research Unit, National institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8634, Japan;(3) Department of Applied Biological Chemistry, School of Agriculture, Kinki University, 3327-204 Nakamachi, Nara 631-8505, Japan;(4) Graduate School of Agriculture, Kyoto University, Kita-shirakawa, Sakyo-Ku, Kyoto 606-8502, Japan;(5) MRC Functional Genetics Unit, Department of Physiology, Anatomy and Genetics, University of Oxford, Le Gros Clark Building, South Parks Road, Oxford , OX1 3QX, UK |
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Abstract: | The low mammalian toxicity of neonicotinoid insecticides has been shown to be attributable, at least in part, to their selective
actions on insect nicotinic acetylcholine receptors (nAChRs). There are multiple nAChRs in insects and a wealth of neonicotinoid
chemicals. Studies to date have discribed a wide range of effects on nAChRs, notably partial agonist, super agonist and antagonist
actions. Both the diversity of the neonicotinoid actions and their selectivity for insect over vertebrate nAChRs are the result
of physicochemical and steric interactions at their molecular targets (nAChRs). In such interactions, the formation and breakage
of hydrogen bond (HB) networks plays a key role. Therefore the loss or gain of even a single HB resulting from either structural
changes in neonicotinoids, or the amino acid sequence of a particular nAChR subunit, could result in a drastic modification
of neonicotinoid actions. In addition to the amino acid residues, the backbone carbonyl of nAChRs may also be involved in
the formation of HB networks with neonicotinoids. |
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