Identification and in silico analysis of antithrombotic peptides from the enzymatic hydrolysates of Tenebrio molitor larvae
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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.
KeywordsTenebrio molitor larvae Antithrombotic peptide Enzymatic hydrolysis Isolation Identification In silico analysis
Reverse-phase liquid chromatography
Liquid chromatography tandem mass spectrometry
Degree of hydrolysis
Discovery Studio 2.5
Analysis of variance
This work was financially supported by the Science and Technology Project of Zhejiang Province, China [grant number LGN19C200018].
Compliance with ethical standards
Conflict of interest
The authors declare no conflict of interest.
Compliance with ethics requirements
This article does not contain any studies with human or animal subjects.
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