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.
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.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2008年第3期542-545,共4页
Chemical Journal of Chinese Universities
基金
国家“八六三”计划(批准号:2006AA102331)资助
