血管紧张素转化酶抑制肽的设计与抗酶解研究
The design of ACE peptides and enzymatic hydrolysis resistance research
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摘要: 设计了血管紧张素转换酶抑制肽（angiotensin converting enzyme inhibitory peptides,ACE抑制肽）,并对设计的ACE抑制肽进行抗酶解研究。选取静电荷和疏水性这两个重要的结构参数,设计了一系列的ACE抑制肽。采用反相高效液相色谱（reversed-phase high performance liquid chromatography,RP-HPLC）来检测37℃下胃蛋白酶和胰蛋白酶对ACE抑制肽的酶解后的保留量,以研究静电荷和疏水性与肽的抗酶解之间的关系。结果表明,肽中疏水性氨基酸含量及蛋白质的平均疏水性均与ACE抑制肽的抗酶解活性呈正相关,而静电荷对ACE抑制肽抗酶解的影响较小。Abstract: The angiotensin converting enzyme inhibitory peptides ( ACE inhibitory peptides) was designed and synthesized in this research, and the enzymatic hydrolysis of the ACE inhibitory peptides was following studied.In this study, antihypertensive peptides derived from peanut protein were made as templates, and net charge and hydrophobicity which were two important structural parameters were selected to design a series of ACE inhibitory peptides.The ACE inhibitory peptides were hydrolyzed by pepsin and trypsin at 37℃ and were monitored by reversed- phase high performance liquid chromatography ( RP- HPLC) . At last, the relationship between the net charge and hydrophobicity of ACE inhibitory peptides and their enzyme-resistant activity was studied.The results showed that the enzyme-resistant activity of ACE inhibitory peptides was significantly and positively correlated with hydrophobicity of peptides.However, the influence of the net charge to enzyme-resistant activity of ACE inhibitory peptides is not significant.
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