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题名: Identification of Angiotensin I-Converting Enzyme Inhibitors in Peptides Mixture of Hydrolyzed Red Deer Plasma with Proteomic Approach
作者: Liu Xiaoyan1, 2;  Song Chunxia1, 2;  Chen Rui1, 2;  Jiang Xinning1, 2;  Jin Yan1;  Zou Hanfa1
关键词: proteomics ;  angiotensin I-converting enzyme ;  inhibitory activity ;  peptides ;  red deer plasma
刊名: CHINESE JOURNAL OF CHEMISTRY
发表日期: 2010-09-01
DOI: 10.1002/cjoc.201090282
卷: 28, 期:9, 页:1665-1672
收录类别: SCI ;  IC
文章类型: Article
WOS标题词: Science & Technology ;  Physical Sciences
类目[WOS]: Chemistry, Multidisciplinary
研究领域[WOS]: Chemistry
英文摘要: Proteomics is a rapidly emerging set of key technologies that are of major importance for proteins and drug development process, especially when mass spectrometry (MS) is being used for high-throughput characterization and identification of proteins. Since the safer and healthier angiotensin I-converting enzyme (ACE) inhibitors are extremely concerned, many research groups have combed for novel ACE inhibitors from food components by different approaches. Here, shotgun proteomics technology aided with structure-activity analysis was applied to screen ACE inhibitory peptides from hydrolyzed red deer plasma. The peptides were analysed by mass spectrometry after primary separation with Sephadex G-25 chromatography. 36 peptides were identified by searching red deer database and 165 peptide sequences derived were identified in mammalian database. Amino acid sequences of peptide and bioactivity relationship have been developed as a faster and useful way to predict and screen new inhibitors. Depending on the relationship of peptide structure and ACE inhibitory activity, a nonapeptide, VYNEGLPAP, was predicted with ACE inhibitory activity. The activity was verified by synthesized VYNEGLPAP and the 50% inhibition concentration (IC(50)) was 3.1 mu mol center dot L(-1). VYNEGLPAP had good thermal stability, pH stability and strong enzyme-resistant properties against gastrointestinal protease. Kinetic experiments demonstrated that inhibitory kinetic mechanism of this peptide was competitive. This study demonstrated the possibility of screening bioactive peptides from protein hydrolysates mixture based on shotgun proteomics technology, which will provide a potential convenient method to screening bioactive peptides from protein source.
关键词[WOS]: SPONTANEOUSLY HYPERTENSIVE-RATS ;  ANTIHYPERTENSIVE PEPTIDES ;  SYNTHETIC PEPTIDES ;  MASS-SPECTROMETRY ;  RENIN-ANGIOTENSIN ;  FOOD PROTEINS ;  RABBIT LUNG ;  PURIFICATION ;  DESIGN ;  DIGESTION
语种: 英语
WOS记录号: WOS:000282998700025
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/141961
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Dalian Univ Technol, Natl Chromatog Res & Anal Ctr, Dalian Inst Chem Phys, Dalian 116023, Liaoning, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China

Recommended Citation:
Liu Xiaoyan,Song Chunxia,Chen Rui,et al. Identification of Angiotensin I-Converting Enzyme Inhibitors in Peptides Mixture of Hydrolyzed Red Deer Plasma with Proteomic Approach[J]. CHINESE JOURNAL OF CHEMISTRY,2010,28(9):1665-1672.
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