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Molecular mechanisms of novel peptides from silkworm pupae that inhibit alpha-glucosidase

文献类型： 外文期刊

作者： Zhang, Yu 1 ; Wang, Nan 2 ; Wang, Wei 1 ; Wang, Junhong 1 ; Zhu, Zuoyi 1 ; Lia, Xue 1 ;

作者机构： 1.Zhejiang Acad Agr Sci, Inst Qual & Stand Agr Prod, Hangzhou, Zhejiang, Peoples R China

2.Zhejiang Shuren Univ, Coll Biol & Environm Engn, Hangzhou 310021, Zhejiang, Peoples R China

3.Minist Agr Agr Prod Qual & Safety, Base State Key Lab, Hangzhou 310021, Zhejiang, Peoples R China

关键词： Molecular mechanism;alpha-glucosidase;In-silico screening;Silkworm pupae

期刊名称：PEPTIDES （ 影响因子：3.75； 五年影响因子：3.389 ）

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收录情况： SCI

摘要： The objectives of this study were to identify peptides that inhibit alpha-glucosidase using a quantitative structure-activity relationship (QSAR) screening method and a database of silkworm peptides. This study compared the docking characteristics of several peptides with high inhibitory activity against alpha-glucosidase and summarized the molecular mechanisms by which the silkworm peptides affected alpha-glucosidase. Four peptides that strongly inhibited alpha-glucosidase were obtained: Gln-Pro-Gly-Arg with IC50 at 65.8 mu mol/L, Ser-Gln-Ser-Pro-Ala at 20 mu mol/L, Gln-Pro-Pro-Thr at 560 mu mol/L and Asn-Ser-Pro-Arg at 205 mu mol/L. Studies docking the peptides to the active site of alpha-glucosidase (PDB ID: 2QMJ) showed that a common characteristic was Lys776 in 2QMJ, which could be a critical target for alpha-glucosidase trapping of inhibitory peptides. The results revealed that the four peptides, especially Ser-Gln-Ser-Pro-Ala, could be potential drugs for treating diabetes. (C) 2015 Elsevier Inc. All rights reserved.

  • 相关文献

[1]Molecular Mechanisms of Several Novel Dipeptides with Angiotensin-I-converting Enzyme Inhibitory Activity from In-silico Screening of Silkworm Pupae Protein. Wang, Wei,Zhang, Yu,Zhu, Zuoyi,Wang, Nan.

[2]A review for the molecular research of russet/semi-russet of sand pear exocarp and their genetic characters. Wang, Yue-zhi,Dai, Mei-song,Cai, Dan-ying,Zhang, Shujun,Shi, Ze-bin.

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