Purification and Characterization of Antiproliferative Peptide from Enzymatic Hydrolysates of Chinese Soft-Shelled Turtle Protein

被引:1
|
作者
Wang, Nan [1 ]
Wang, Wei [2 ]
Liu, Xiaoxiang [3 ]
Liu, Caiqin [1 ]
Jin Jiancang [1 ]
Lu, Yin [1 ]
机构
[1] Zhejiang Shuren Univ, Coll Biol & Environm Engn, Hangzhou 310021, Zhejiang, Peoples R China
[2] Zhejiang Acad Agr Sci, Inst Qual & Standard Agr Prod, Hangzhou 310021, Zhejiang, Peoples R China
[3] Hangzhou Med Coll, Fac Basic Med, Hangzhou 310053, Zhejiang, Peoples R China
基金
中国国家自然科学基金;
关键词
Antiproliferative activity; Peptide; Chinese soft-shelled turtle; Enzymatic hydrolysis; Q-TOF MS/MS; ANTIOXIDATIVE PEPTIDE; ANTICANCER; APOPTOSIS; INDUCTION; MUSCLE; CELLS;
D O I
10.17957/IJAB/15.0521
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Chinese soft-shelled turtle protein was hydrolyzed using neutrase to produce antiproliferative peptides. To identify the antiproliferative peptides, Chinese soft-shelled turtle protein hydrolysate was fractionated by Sephadex G-25. Antiproliferative activities of the identified peptides were evaluated using the MTT assay. Three novel antiproliferative peptides were identified as Asp-Glu-Gla-Asp-Leu-Leu-Gla (MW: 745.79 Da), Glu-Gla-Gly-Val-Asn-Asp-Trp (MW: 789.81 Da), and Gly-Ger-IleGer-Ger-Gly-Gln-Val (MW: 733.78 Da). These peptides with exhibited antiproliferative activity on A549 cancer cells with IC50 values of 129.12 +/- 4.21, 150.89 +/- 3.75 and 142.47 +/- 5.12 mu g/mL, respectively. This bioactivity was likely due to the small size of the peptides and the peptide sequences have hydrophobic amino acids. Further investigations were suggested on larger scale employing standard procedures. (C) 2018 Friends Science Publishers
引用
收藏
页码:209 / 214
页数:6
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