Angiotensin I-converting enzyme inhibitory peptides: Inhibition mode, bioavailability, and antihypertensive effects

被引:116
作者
Jao, Chia-Ling [1 ]
Huang, Shih-Li [2 ]
Hsu, Kuo-Chiang [3 ]
机构
[1] Tung Fang Design Univ, Dept Food & Beverage Management, Kaohsiung 82941, Taiwan
[2] Natl Kaohsiung Univ Hospital & Tourism, Dept Baking Technol & Management, Kaohsiung 81271, Taiwan
[3] China Med Univ, Dept Nutr, 91 Hsueh Shih Rd, Taichung 40402, Taiwan
来源
BIOMEDICINE-TAIWAN | 2012年 / 2卷 / 04期
关键词
ACE inhibitory peptide; antihypertensive effect; bioavailability; gastrointestinal digestion; inhibition mode;
D O I
10.1016/j.biomed.2012.06.005
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
Bioactive peptides within the original food-derived proteins are inactive but can be activated by releasing them during food processing (by enzymatic hydrolysis or fermentation) or during gastrointestinal (GI) digestion. Among all the bioactive peptides, the antihypertensive peptides attract particular attention owing to the prevalence of high blood pressure, which plays an important role in cardiovascular diseases. These peptides have the ability to act as angiotensin I-converting enzyme (ACE) inhibitors. Previous studies have shown that the ACE inhibitory peptides functioned as competitive, noncompetitive, or uncompetitive inhibitors, and therefore, the structure-activity relationship of the peptides with various inhibition modes needs to be clarified. Besides, the ACE inhibitory activity of these peptides in vitro does not always suggest its antihypertensive effect in vivo, which is based on its fate to encounter GI enzymes and brush-border membrane peptidases, after oral administration. This paper reviews the current literature on ACE inhibitory peptides, focusing on the structure-activity relationship and inhibition mechanisms due to their inhibition modes. In addition, the in vitro-simulated GI digestion for assessing bioavailability and in vivo antihypertensive effects of the peptides are also summarized. Copyright (C) 2012, China Medical University. Published by Elsevier Taiwan LLC. All rights reserved.
引用
收藏
页码:130 / 136
页数:7
相关论文
共 54 条
[1]   ESSENTIAL HYPERTENSION - RENIN AND ALDOSTERONE, HEART ATTACK AND STROKE [J].
BRUNNER, HR ;
BUHLER, FR ;
BARD, RH ;
BAER, L ;
GOODWIN, FT ;
NEWTON, MA ;
KRAKOFF, LR ;
LARAGH, JH .
NEW ENGLAND JOURNAL OF MEDICINE, 1972, 286 (09) :441-+
[2]   Angiotensin I-converting enzyme inhibitor from Grifola frondosa [J].
Choi, HS ;
Cho, HY ;
Yang, HC ;
Ra, KS ;
Suh, HJ .
FOOD RESEARCH INTERNATIONAL, 2001, 34 (2-3) :177-182
[3]   The antihypertensive effect of peptides: A novel alternative to drugs? [J].
Fang Hong ;
Luo Ming ;
Sheng Yi ;
Li Zhanxia ;
Wu Yongquan ;
Liu Chi .
PEPTIDES, 2008, 29 (06) :1062-1071
[4]   ISOLATION OF BRADYKININ-POTENTIATING PEPTIDES FROM BOTHROPS-JARARACA VENOM [J].
FERREIRA, SH ;
BARTELT, DC ;
GREENE, LJ .
BIOCHEMISTRY, 1970, 9 (13) :2583-&
[5]  
FitzGerald RJ, 2000, BRIT J NUTR, V84, pS33
[6]  
Fujita H, 2000, J FOOD SCI, V65, P564, DOI 10.1111/j.1365-2621.2000.tb16049.x
[7]   Production of angiotensin-I-converting-enzyme-inhibitory peptides in fermented milks started by Lactobacillus delbrueckii subsp bulgaricus SS1 and Lactococcus lactis subsp cremoris FT4 [J].
Gobbetti, M ;
Ferranti, P ;
Smacchi, E ;
Goffredi, F ;
Addeo, F .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2000, 66 (09) :3898-3904
[8]   Isolation of angiotensin I converting enzyme (ACE) inhibitor from fermented oyster sauce, Crassostrea gigas [J].
Je, JY ;
Park, JY ;
Jung, WK ;
Park, PJ ;
Kim, SK .
FOOD CHEMISTRY, 2005, 90 (04) :809-814
[9]   Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats [J].
Jung, WK ;
Mendis, E ;
Je, JY ;
Park, PJ ;
Son, BW ;
Kim, HC ;
Choi, YK ;
Kim, SK .
FOOD CHEMISTRY, 2006, 94 (01) :26-32
[10]  
Kearney PM, 2005, LANCET, V365, P217, DOI 10.1016/S0140-6736(05)70151-3