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A convenient total synthesis of (Z)-12-tetradecenyl acetate (1a) and (E)-12-tetradecenyl acetate (1b), which are the sex pheromones of Ostrinia furnacalis (Guenée), has been achieved. The target mixture molecules, of a cis-to-trans-isomer ratio of 27 to 73, were synthesized in 40% overall yield and through [13C + 1C] synthetic strategy in five steps from commercially available and cheap industrial brassylic acid as key starting material. The electroantennogram (EAG) responses of synthetic sex pheromone to ACB male moths were conducted. The results showed that the target mixture molecules were found to have a good activity and displayed significantly stronger EAG responses ranging from 10 to 1000 g, and the optimized stimulating dosage of the activity of synthetic sex pheromone to ACB males is 10 g. Compared with the existing routes, this synthetic approach is operationally simple, goodyielding, and cost-effective, which could serve as a basis for developing the techniques of sex pheromone mass trapping or mating disruption and providing an environmentally benign method to control ACB pests.

Motivation Phosphate binding plays an important role in modulating protein-protein interactions, which are ubiquitous in various biological processes. Accurate prediction of phosphate binding sites is an important but challenging task. Small size and diversity of phosphate binding sites lead to a substantial challenge for developing accurate prediction methods. Results Here we present the phosphate binding site predictor (PBSP), a novel and accurate approach to identifying phosphate binding sites from protein structures. PBSP combines an energy-based ligand-binding sites identification method with reverse focused docking using a phosphate probe. We show that PBSP outperforms not only general ligand binding sites predictors but also other existing phospholigand-specific binding sites predictors. It achieves ∼95% success rate for top 10 predicted sites with an average Matthews correlation coefficient (MCC) value of 0.84 for successful predictions. PBSP can accurately predict phosphate binding modes, with average position error of 1.4 Å and 2.4 Å in bound and unbound datasets, respectively. Lastly, visual inspection of the predictions is conducted. Reasons for failed predictions are further analyzed and possible ways to improve the performance are provided. These results demonstrate a novel and accurate approach to phosphate binding sites identification in protein structures. Availability The software and benchmark datasets are freely available at http://web.pkusz.edu.cn/wu/PBSP/. Supplementary information Supplementary data are available at Bioinformatics online.