Chem. J. Chinese Universities

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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

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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