Primary and secondary structure of novel ACE-inhibitory peptides from egg white protein.
Primary and secondary structure of novel ACE-inhibitory peptides from egg white protein.
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DOI：
10.1016/j.foodchem.2012.01.032
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发表时间：
2012-07
期刊：
影响因子：
8.8
通讯作者：
Zhipeng Yu;Boqun Liu;Wenzhu Zhao;Yongguang Yin;Jingbo Liu;Feng Chen
中科院分区：
文献类型：
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作者：
Zhipeng Yu;Boqun Liu;Wenzhu Zhao;Yongguang Yin;Jingbo Liu;Feng Chen
研究了新型蛋清蛋白血管紧张素转换酶(ACE)抑制肽的一级结构，首次探索了该多肽的二级结构。从ACE抑制活性、抗氧化活性和抗凝血活性三个方面对生物活性多肽的潜在作用进行了生物活性筛选。用LC串联质谱法对蛋清蛋白中的生物活性多肽进行了表征，并用傅立叶变换红外光谱对其二级结构进行了研究。结果表明，用LC/MS/MS鉴定了11个生物活性多肽，其中3个为新结构，8个为已知结构，并用Fmoc固相法合成。Thr-Asn-Gly-Ile-Arg多肽(TNGIIR)对血管紧张素转换酶有较强的抑制活性。抑制血管紧张素转换酶活性50%所需的多肽TNGIIR的浓度为70μM。由此可见，多肽的一级和二级结构可能具有抑制血管紧张素转换酶活性的作用。
The primary structure of novel angiotensin converting enzyme (ACE) inhibitory peptide from egg white protein was investigated, and secondary structure of the peptide was explored for the first time. The potential effects of bioactive peptides were submitted to bioactivity screening with ACE inhibitory activity, antioxidant property, and anticoagulation activity. Bioactive peptides from egg white protein were characterized by LC tandem mass spectrometric, and secondary structures of those peptides were investigated by FT-IR. Our results showed that total 11 bioactive peptides with three new and eight known structures were identified with LC/MS/MS, which then were synthesized by Fmoc solid phase method. Peptide Thr-Asn-Gly-Ile-Ile-Arg (TNGIIR) exhibited higher activity against ACE to other two new peptides. The concentration of the peptide TNGIIR, necessary to inhibit 50% the activity of ACE was 70μM. Results also suggested that the secondary structural differences between peptides could also influence the ACE inhibition capacity. Thus, it appears that primary and secondary structure of peptide plays the potential role inhibiting the ACE activity.