Novel casein-derived peptides with antihypertensive activity
Novel casein-derived peptides with antihypertensive activity
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DOI：
10.1016/j.idairyj.2009.05.004
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发表时间：
2009-10-01
影响因子：
3.1
通讯作者：
Recio, Isidra
中科院分区：
文献类型：
--
作者：
del Mar Contreras, Maria;Carron, Rosalia;Recio, Isidra
在这项研究中，我们报告了新的酪蛋白衍生肽序列与血管紧张素转换酶（ACE）抑制活性和抗高血压活性证明在自发性高血压大鼠（SHR）。用胃蛋白酶水解总酪蛋白得到肽。为了鉴定ACE抑制肽，酪蛋白水解物通过半制备高效液相色谱法分级分离，并通过使用离子阱质谱仪对活性级分中所含的44个（CN）肽进行测序。在已鉴定的肽中。对应于α（s1）-CN f（90-94）（RYLGY）、α（s1）-CN f（143-149）（AYFYPEL）和α（s2）-CN f（89-95）（YQKFPQY）的三个序列显示出IC 50值分别低至0.71 μ M、6.58 μ M和20.08 μ M。当以5 mg/kg体重的剂量口服给SHR时，这三种肽也表现出抗高血压活性。肽RYLGY和AYFYPEL在SHR中的活性与以相同剂量口服给药时三肽VPP所发现的活性相似。(C)2009爱思唯尔有限公司保留所有权利。
In this study, we report novel casein-derived peptide sequences with angiotensin converting enzyme (ACE)-inhibitory activity and antihypertensive activity demonstrated in spontaneously hypertensive rats (SHR). The peptides were obtained by enzymatic hydrolysis of total isoelectric casein with pepsin. To identify ACE-inhibitory peptides, the casein hydrolysate was fractionated by semi-preparative high performance liquid chromatography, and 44 (CN) peptides contained in the active fractions were sequenced by using an ion trap mass spectrometer. Among the identified peptides. three sequences, that corresponded to alpha(s1)-CN f(90-94) (RYLGY), alpha(s1)-CN f(143-149) (AYFYPEL), and alpha(s2)-CN f(89-95) (YQKFPQY), showed IC50 values as low as 0.71 mu M, 6.58 mu M, and 20.08 mu M, respectively. These three peptides also exerted anti hypertensive activity when they were orally administered to SHR at a dose of 5 mg kg(-1) of body weight. The activity of peptides RYLGY and AYFYPEL in SHR was similar to that found for tripeptide VPP when orally administered at the same dose. (C) 2009 Elsevier Ltd. All rights reserved.