The ryanodine receptor (RyR) is an intracellular calcium channel critical to the regulation of insect muscle contraction and the target site of diamide insecticides such as chlorantraniliprole, cyantraniliprole and flubendiamide. To-date, diamides are the only known class of synthetic molecules with high potency against insect RyRs. Target-based screening of an informer library led to discovery of a novel class of RyR activators, pyrrole-2-carboxamides. Efforts to optimize receptor activity resulted in analogs with potency comparable to that of commercial diamides when tested against RyR of the fruit fly, Drosophila melanogaster. Surprisingly, testing of pyrrole-2-carboxamides in whole-insect screens showed poor insecticidal activity, which is partially attributed to differential selectivity among insect receptors and rapid detoxification.

Among various lepidopteran species field resistance to diamide insecticides has been well documented and in many cases has been attributed to a single point mutation, G4946E, of the RyR gene. As with diamide insecticides, the G4946E mutation confers greatly reduced sensitivity to pyrrole-2-carboxamides. This, coupled with findings from radioligand binding studies, indicates a shared binding domain between anthranilic diamides and pyrrole-2-carboxamides.

ryanodine受体（RyR）是细胞内的钙离子通道，对调节昆虫的肌肉收缩和双酰胺杀虫剂（如绿丹腈，氰基腈和氟苯二酰胺）的目标部位至关重要。迄今为止，二酰胺是唯一已知的一类对昆虫RyR具有高效力的合成分子。基于目标的信息库筛选导致发现一类新型的RyR激活剂吡咯2-羧酰胺。当针对果蝇果蝇的RyR进行测试时，优化受体活性的努力产生了与商用二酰胺类似的效力。。出乎意料的是，在全昆虫筛选中测试吡咯-2-羧酰胺显示出较差的杀虫活性，这部分归因于昆虫受体之间的选择性差异和快速排毒。

在各种鳞翅目物种中，对二酰胺杀虫剂的田间抗药性已得到充分证明，并且在许多情况下归因于RyR基因的单点突变G4946E。与二酰胺类杀虫剂一样，G4946E突变使对吡咯-2-羧酰胺的敏感性大大降低。这与放射性配体结合研究的结果相结合，表明在邻氨基苯甲酰胺和吡咯-2-羧酰胺之间有一个共享的结合结构域。