Identification of Angiotensin I-Converting Enzyme Inhibitors in Peptides Mixture of Hydrolyzed Red Deer Plasma with Proteomic Approach
文献类型:期刊论文
作者 | Liu Xiaoyan1,2; Song Chunxia1,2; Chen Rui1,2; Jiang Xinning1,2; Jin Yan1; Zou Hanfa1 |
刊名 | chinese journal of chemistry
![]() |
出版日期 | 2010-09-01 |
卷号 | 28期号:9页码:1665-1672 |
关键词 | proteomics angiotensin I-converting enzyme inhibitory activity peptides red deer plasma |
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. |
WOS标题词 | science & technology ; physical sciences |
类目[WOS] | chemistry, multidisciplinary |
研究领域[WOS] | chemistry |
关键词[WOS] | spontaneously hypertensive-rats ; antihypertensive peptides ; synthetic peptides ; mass-spectrometry ; renin-angiotensin ; food proteins ; rabbit lung ; purification ; design ; digestion |
收录类别 | SCI ; IC |
语种 | 英语 |
WOS记录号 | WOS:000282998700025 |
公开日期 | 2015-11-17 |
源URL | [http://159.226.238.44/handle/321008/141961] ![]() |
专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
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 |
推荐引用方式 GB/T 7714 | 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. |
APA | Liu Xiaoyan,Song Chunxia,Chen Rui,Jiang Xinning,Jin Yan,&Zou Hanfa.(2010).Identification of Angiotensin I-Converting Enzyme Inhibitors in Peptides Mixture of Hydrolyzed Red Deer Plasma with Proteomic Approach.chinese journal of chemistry,28(9),1665-1672. |
MLA | Liu Xiaoyan,et al."Identification of Angiotensin I-Converting Enzyme Inhibitors in Peptides Mixture of Hydrolyzed Red Deer Plasma with Proteomic Approach".chinese journal of chemistry 28.9(2010):1665-1672. |
入库方式: OAI收割
来源:大连化学物理研究所
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。