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Dipeptidyl peptidase IV inhibitory peptides from Chlorella vulgaris: in silico gastrointestinal hydrolysis and molecular mechanism

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Abstract

Chlorella vulgaris: is a nutritional food with high protein content. Thus, 43 protein sequences from C. vulgaris were in silico gastrointestinal digested with the aid of BIOPEP. A peptide library of 468 di- and tri-peptides was built from the produced peptides. Six peptides, AAR, VPA, VPW, IPL, IPR, and PPL, were selected for DPP-IV inhibitory assay based on their sequence feature with Pro or Ala at the second N-terminal site. VPA, VPW, IPL, and IPR had potency of DPP-IV inhibition. VPW and IPR with the same N-terminal and second N-terminal sites as those of diprotin A (IPI) and diprotin B (VPL) achieved relative inhibitory IC50 value of 6.4 and 6.9 versus IPI. These peptides were further demonstrated gastrointestinal stable in vitro and could also inhibit the DPP-IV in mouse serum. Molecular docking illustrated the inhibitory mechanism of VPW and IPR. Both VPW and IPR binding with DPP-IV through hydrogen bonds, van Edward Mars interactions, and hydrophobic interactions. However, VPW formed more stable interaction with DPP-IV. The results suggested that C. vulgaris proteins would be a good source for DPP-IV inhibitory peptides.

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Acknowledgements

This work was supported by the “National Natural Science Foundation of China (No. 31301413)”, “Open Funding Project of the State Key Laboratory of Bioreactor Engineering”, and “National Basic Research Program of China (No. 2012CB721103)”.

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Authors and Affiliations

  1. State Key Laboratory of Bioreactor Engineering, Department of Food Science and Technology, School of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 283, Shanghai, 200237, People’s Republic of China

    Qiaosha Zhu, Xujun Chen, Junjie Wu, Yan Zhou, Ming Fang, Jingli Xie & Dongzhi Wei

  2. Department of Radiotherapy of Zhongshan Hospital, Fudan University, Shanghai, 200032, People’s Republic of China

    Yang Qian

  3. Shanghai Collaborative Innovation Center for Biomanufacturing (SCICB), Shanghai, 200237, People’s Republic of China

    Jingli Xie & Dongzhi Wei

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  1. Qiaosha Zhu
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Correspondence to Jingli Xie.

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Zhu, Q., Chen, X., Wu, J. et al. Dipeptidyl peptidase IV inhibitory peptides from Chlorella vulgaris: in silico gastrointestinal hydrolysis and molecular mechanism. Eur Food Res Technol 243, 1739–1748 (2017). https://doi.org/10.1007/s00217-017-2879-1

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  • DOI: https://doi.org/10.1007/s00217-017-2879-1

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