A novel angiotensin-I converting enzyme (ACE) inhibitory peptide from gastrointestinal protease hydrolysate of silkworm pupa (Bombyx mori) protein: Biochemical characterization and molecular docking study

文献类型: 外文期刊

第一作者: Wu, Qiongying

作者: Wu, Qiongying;Jia, Junqiang;Yan, Hui;Du, Jinjuan;Gui, Zhongzheng;Wu, Qiongying;Jia, Junqiang;Yan, Hui;Gui, Zhongzheng

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关键词: Silkworm pupa (Bombyx mori);ACE inhibitory peptide;Gastrointestinal protease;Inhibition pattern;Molecular docking

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: Silkworm pupa (Bombyx mori) protein was hydrolyzed using gastrointestinal endopeptidases (pepsin, trypsin and alpha-chymotrypsin). Then, the hydrolysate was purified sequentially by ultrafiltration, gel filtration chromatography and RP-HPLC. A novel ACE inhibitory peptide, Ala-Ser-Leu, with the IC50 value of 102.15 mu M, was identified by IT-MS/MS. This is the first report of Ala-Ser-Leu from natural protein. Lineweaver-Burk plots suggest that the peptide is a competitive inhibitor against ACE. The molecular docking studies revealed that the ACE inhibition of Ala-Ser-Leu is mainly attributed to forming very strong hydrogen bonds with the S1 pocket (A1a354) and the S2 pocket (G1n281 and His353). The results indicate that silkworm pupa (B. mori) protein or its gastrointestinal protease hydrolysate could be used as a functional ingredient in auxiliary therapeutic foods against hypertension. (C) 2014 Elsevier Inc. All rights reserved.

分类号: Q5

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