کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2075715 | 1544909 | 2012 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Angiotensin I-converting enzyme inhibitory peptides: Inhibition mode, bioavailability, and antihypertensive effects
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوتکنولوژی یا زیستفناوری
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: BioMedicine - Volume 2, Issue 4, December 2012, Pages 130-136
Journal: BioMedicine - Volume 2, Issue 4, December 2012, Pages 130-136
نویسندگان
Chia-Ling Jao, Shih-Li Huang, Kuo-Chiang Hsu,