QIGLF, a novel angiotensin I-converting enzyme-inhibitory peptide from egg white protein.
QIGLF, a novel angiotensin I-converting enzyme-inhibitory peptide from egg white protein.
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DOI：
10.1002/jsfa.4266
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发表时间：
2011-03
影响因子：
4.1
通讯作者：
Zhipeng Yu;Wenzhu Zhao;Jingbo Liu;Jing Lu;Feng Chen
中科院分区：
文献类型：
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作者：
Zhipeng Yu;Wenzhu Zhao;Jingbo Liu;Jing Lu;Feng Chen
应用液相色谱/串联质谱法（LC/MS/MS）可以从鸡蛋白色蛋白中快速筛选新型血管紧张素I转化酶（ACE）抑制肽。本研究以鸡蛋白色蛋白为原料，采用Alcalase酶解法制备了几种ACE抑制活性较强的多肽，经Sephadex G25柱纯化后，用LC/MS/MS进行鉴定，并用圆二色谱（CD）进行结构分析。结果进一步研究了显示ACE抑制活性的肽序列DHPFLF、HAEIN和QIGLF在胃肠道溶液中的稳定性和在溶液混合物中的二级结构变化。QIGLF表现出最高的活性（IC（50）=75 µmol L（-1）），并且对胃肠道蛋白酶的消化具有抗性。QIGLF的圆二色性光谱表明存在α-螺旋构象。结论经LC/MS/MS鉴定3个肽段，并采用Fmoc固相合成法合成。在这三个序列中，只有肽序列QIGLF是潜在的ACE抑制剂，IC（50）值为75 µmol L（-1）。此外，QIGLF表现出较低的胃肠道酶敏感性，并含有相对较高量的α-螺旋。
BACKGROUND Novel angiotensin I-converting enzyme (ACE)-inhibitory peptides from egg white protein can be rapidly screened by liquid chromatography/tandem mass spectrometry (LC/MS/MS). In this study, several peptides with higher ACE-inhibitory activity were prepared from egg white protein by enzymatic hydrolysis with Alcalase, purified with Sephadex G25, identified by LC/MS/MS and their structure determined by circular dichroism (CD) spectroscopy. RESULTS Peptide sequences DHPFLF, HAEIN and QIGLF that showed ACE-inhibitory activity were investigated further for their stability in gastrointestinal solution and for changes in their secondary structure in solution mixtures. QIGLF exhibited the highest activity (IC(50)=75 µmol L(-1)) and was resistant to digestion by proteases of the gastrointestinal tract. The CD spectrum of QIGLF showed the presence of the α-helix conformation. CONCLUSION Three peptides were identified by LC/MS/MS and synthesised by Fmoc solid phase synthesis. Of the three, only the peptide sequence QIGLF was a potential ACE inhibitor, with an IC(50) value of 75 µmol L(-1) . Moreover, QIGLF showed low gastrointestinal enzyme susceptibility and contained a relatively high amount of α-helix.