牦牛乳干酪苦味肽ACE抑制活性表征的分子机制
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(甘肃农业大学食品科学与工程学院 甘肃省功能乳品工程实验室 兰州 730070)

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杨保军(1995—),男,硕士生

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国家自然科学基金项目(31660468)


Molecular Mechanism of ACE Inhibitory Activity Characterization of Yak Milk Cheese Bitter Peptide
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(Functional Dairy Product Engineering Laboratory of Gansu, College of Food Science and Engineering,Gansu Agricultural University, Lanzhou 730070)

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    摘要:

    用生物信息学方法计算并分析牦牛乳硬质干酪中鉴定出的3种苦味肽RK7、VN10和SN12的理化特性,对肽结构做能量最小化处理,从PDB数据库获取血管紧张素转化酶(ACE)蛋白晶体的X射线衍射三维结构,通过分子对接和数据库比对评估和表征苦味肽的ACE抑制活性及其与ACE的作用机理。通过计算得出RK7、VN10和SN12的不稳定性指数分别为19.84,49.44和42.87,疏水性分别为42.86%,70.00%和66.67%。分子对接结果表明:ACE分子中的Ala356、His387、Phe391、Pro407、His410、Glu411、Ser517、Val518、Pro519残基为其与RK7和VN10结合的重要活性位点,RK7、VN10和SN12分别与ACE活性位点的氨基酸形成3,2个和0个氢键;RK7、VN10和SN12与ACE的结合表现出相似的分子机制,均结合于ACE的活性空腔内(X:35.46,Y:43.15,Z:55.47,R:9 ?魡);RK7、VN10和SN12与BIOPEP数据库中已知ACE抑制肽的最高相似度分别为57.14%,90.00%和75.00%。综合RK7、VN10和SN12与ACE活性位点氨基酸残基相互作用的情况和BIOPEP数据库比对结果预测出3种肽段的ACE抑制活性:VN10 > RK7 > SN12。本试验为理论层面和分子水平研究干酪苦味肽的ACE抑制活性提供参考。

    Abstract:

    The aim of the experiment was to calculate and analyze the physicochemical properties of three bitter peptides RK7, VN10 and SN12 identified in yak milk hard cheese using bioinformatics methods, and minimize the energy of the peptide structure. Obtained the X-ray diffraction three-dimensional structure of ACE protein crystals from the PDB database, and evaluated and characterized the ACE inhibitory activity of bitter peptides and the mechanism of action with ACE through molecular docking and database comparison. The instability indexes of RK7, VN10 and SN12 were 19.84, 49.44 and 42.87, respectively, and the hydrophobicities were 42.86%, 70.00% and 66.67%, respectively. These three peptides were molecularly docked with ACE, the results of the study showed that the Ala356, His387, Phe391, Pro407, His410, Glu411, Ser517, Val518, and Pro519 residues in the ACE molecule were important active sites for binding to RK7 and VN10, RK7, VN10 and SN12, respectively formed 3, 2 and 0 hydrogen bonds with the amino acids in the active site of ACE. The binding of RK7, VN10 and SN12 to ACE showed similar molecular mechanisms, all of which were bound in the active cavity of ACE(X: 35.46, Y: 43.15, Z: 55.47, R: 9 ?魡). The highest similarities between RK7, VN10 and SN12 and the known ACE inhibitor peptides in the BIOPEP database were 57.14%, 90.00% and 75.00%, respectively. Integrating the interaction of RK7, VN10 and SN12 with the amino acid residues of the active site of ACE and the BIOPEP database comparison results predicted the ACE inhibitory activity of the three peptides: VN10 > RK7 > SN12. Therefore, this experiment provided the reference for studying the ACE inhibitory activity of cheese bitter peptides at the theoretical and molecular levels.

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杨保军,梁琪,宋雪梅.牦牛乳干酪苦味肽ACE抑制活性表征的分子机制[J].中国食品学报,2022,22(5):8-17

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  • 收稿日期:2021-12-31
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  • 在线发布日期: 2022-06-15
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