高等学校化学学报

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血红蛋白片段的合成及生物活性

李晓晖1, 袁恒立1, 胡建恩2, 修志龙1   

    1. 大连理工大学环境与生命学院生物科学与工程系, 大连 116024;
    2. 中国科学院大连化学物理研究所, 大连 116023
  • 收稿日期:2007-07-01 修回日期:1900-01-01 出版日期:2008-03-10 发布日期:2008-03-10
  • 通讯作者: 李晓晖

Synthesis and Biological Activities of Hemoglobin Fragments

LI Xiao-Hui1*, YUAN Heng-Li1, HU Jian-En2, XIU Zhi-Long1   

    1. Department of Bioscience and Biotechnology, School of Environmental and Biological Science and Technology, Dalian University of Technology, Dalian 116024, China;
    2. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China
  • Received:2007-07-01 Revised:1900-01-01 Online:2008-03-10 Published:2008-03-10
  • Contact: LI Xiao-Hui

摘要: 采用多肽固相合成方法, 以Wang 树脂为载体, Fmoc为N-端氨基酸保护基, HOBt-HBTU为缩合试剂, 合成了一系列血红蛋白α链的片段, 产物经RP-HPLC和质谱进行了确定. 生物活性研究结果表明, 该系列多肽具有较高的血管紧张素Ⅰ转换酶抑制活性, 但不具有α-葡萄糖苷酶抑制活性.

关键词: 血红蛋白片段, 多肽固相合成, 血管紧张素Ⅰ转换酶(ACE), α-葡萄糖苷酶

Abstract: The peptides can be obtained by enzymatic proteolysis of food proteins and may act as potential physiological regulators of metabolism during the intestinal digestion of diet. To investigate bioactive peptides within food proteins, six peptides derived from α-chain of hemoglobin were synthesized via peptide solid-phase method. The peptides were purified on Sephadex LH-20 gel chromatography column and detected by RP-HPLC and MS respectively. In vitro bioactivity of Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Phe-Pro-His-Phe showed similar activity(IC50=4.76 μmol/L) in inhibition of angiotensin I-converting enzyme(ACE) compared with that obtained from globin hydro-lysis(IC50=4.92 μmol/L). These results confirm that the peptide inhibitors of ACE, which contain a hydrophobic amino acid at C-terminal with branched side chain(e.g. Leu, Phe, Pro), are more active. No α-glucosidase inhibitory activity was detected. The results indicate that these peptides have a potential antihypertensive effect and possible application in remedy of hypertension

Key words: Hemoglobin fragments, Solid-phase synthesis peptides, Angiotensin I-converting enzyme(ACE), α-Glucosidase

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