Systemic screening of milk protein-derived ACE inhibitors through a chemically synthesised tripeptide library

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• 作者：Fazheng Ren^a ; ^b ; ^c ; Shunliang Zhang^a ; ^b ; ^c ; Huiyuan Guo^a ; ^b ; ^c ; Lu Jiang ; ^a ; ^b ; ^c ; ^{lujiang_edu@yahoo.cn"" rel=""nofollow}
• 关键词：Angiotensin converting enzyme ; Tripeptide library ; System screening ; Solid-phase synthesis
• 刊名：Food Chemistry
• 出版年：2011
• 出版时间：1 October 2011
• 年：2011
• 卷：128
• 期：3
• 页码：761-768
• 全文大小：295 K

文摘

A tripeptide library consisting of 373 tripeptides (nine repeats) based on bovine α-S1 casein and β-lactoglobulin was synthesised chemically, purified by HPLC and the angiotensin-converting enzyme (ACE) inhibitory activities were assayed. Of the 364 tripeptides assayed, 144 showed a relative ACE inhibitory activity higher than 50 % and 43 higher than 60 % , at a set concentration of 2.5 mM. More potent tripeptides were found from α-S1 casein than from β-lactoglobulin. The high percentage of Pro/Tyr in caseins could be the reason for this. Fifteen tripeptides with relative activities higher than 50 % were selected and assayed for their IC₅₀, using hippuryl-l-histidyl-l-leucine as the substrate. The most potent peptide showed an IC₅₀ of 0.85 μM.