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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Quantitative Structure-Activity Relationship Modeling Coupled with Molecular Docking Analysis in Screening of Angiotensin I-Converting Enzyme Inhibitory Peptides from Qula Casein Hydrolysates Obtained by Two-Enzyme Combination Hydrolysis
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Quantitative Structure-Activity Relationship Modeling Coupled with Molecular Docking Analysis in Screening of Angiotensin I-Converting Enzyme Inhibitory Peptides from Qula Casein Hydrolysates Obtained by Two-Enzyme Combination Hydrolysis

机译：通过双酶组合水解获得的QuaTOSIN I转换酶抑制酶抑制酶抑制酶抑制作用的定量结构 - 活性关系建模

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摘要

In this study, Qula casein derived from yak milk casein was hydrolyzed using a two-enzyme combination approach, and high angiotensin I-converting enzyme (ACE) inhibitory activity peptides were screened by quantitative structure-activity relationship (QSAR) modeling integrated with molecular docking analysis. Hydrolysates (3 kDa) derived from combinations of thermolysin + alcalase and thermolysin + proteinase K demonstrated high ACE inhibitory activities. Peptide sequences in hydrolysates derived from these two combinations were identified by liquid chromatography tandem mass spectrometry (LC-MS/MS). On the basis of the QSAR modeling prediction, a total of 16 peptides were selected for molecular docking analysis. The docking study revealed that four of the peptides (KFPQY, MPFPKYP, MFPPQ, and QWQVL) bound the active site of ACE. These four novel peptides were chemically synthesized, and their IC50 was determined. Among these peptides, KFPQY showed the highest ACE inhibitory activity (IC50 = 12.37 +/- 0.43 mu M). Our study indicated that Qula casein presents an excellent source to produce ACE inhibitory peptides.
机译：在本研究中，使用双酶组合方法水解源自牦牛乳酪蛋白的Qula酪蛋白，通过与分子对接集成的定量结构 - 活性关系（QSAR）建模筛选了高血管紧张素I-转换酶（ACE）抑制活性肽分析。水解衍生物（＆ 3kDa）衍生自热溶胶+ alcalase和散热液+蛋白酶K的组合，证明了高ACE抑制活性。通过液相色谱串联质谱（LC-MS / MS）鉴定衍生自用于这两种组合的水解产物中的肽序列。在QSAR建模预测的基础上，选择总共16个肽用于分子对接分析。对接研究表明，四种肽（KFPQY，MPFPKYP，MFPPQ和QWQVL）绑定了ACE的活动位点。将这四种新型肽化学合成，并测定它们的IC 50。在这些肽中，KFPQY显示出最高的ACE抑制活性（IC50 = 12.37 +/-0.43μm）。我们的研究表明，Qula酪蛋白呈现出优异的来源以产生ACE抑制肽。

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