Identification and in silico analysis of antithrombotic peptides from the enzymatic hydrolysates of Tenebrio molitor larvae

• DOI: 10.1007/s00217-019-03381-2
• Publication Date: 2019-10-17T15:25:08Z
• Authors: Fangyuan Chen; Han Jiang; Yongbo Lu; Wenwei Chen; Guangrong Huang
• Keywords: Ion chromatography

Tenebrio molitor is an excellent source of high-quality protein that produces various bioactive peptides. It is a traditional Chinese herbal medicine which has the effect of “activating blood and dissolving stasis”. It aimed to obtain antithrombotic peptides from the Tenebrio molitor larvae hydrolysate generated by treatment with pepsin and trypsin. The hydrolysate was subjected to ion exchange chromatography and gel filtration chromatography; the obtained antithrombotic activity values of the fractions were 40.87% and 65.61% at 8.0 mg/mL, respectively. After further preparation by reverse-phase liquid chromatography, the peptides with antithrombotic activity of 28.66% at 0.2 mg/mL were identified by liquid chromatography tandem mass spectrometry as SLVDAIGMGP and AGFAGDDAPR. Both of the peptides were shown to be nontoxic and could interact with thrombin exosite 1 by molecular docking. These results indicate that peptides from Tenebrio molitor might be used as potential antithrombotic components in the future.