人工抗氧化肽的设计、表达纯化及功能表征

Design, Expression, Purification and Functional Characterization of Artificial Antioxidant Peptides

摘要:

为获得具有抗氧化功能的寡肽，人工设计了3条由不同寡肽串联组成的含胰蛋白酶切割位点的多肽序列，分别命名为ATO、ATW和WIT，并在E. coli BL21（DE3）宿主中实现可溶性表达。纯化的多肽经过胰蛋白酶处理得到3种多肽水解物，体外抗氧化性功能评价实验表明，3种多肽水解物均对不同自由基具有清除作用，其中ATW多肽水解物抗氧化性最强，对DPPH自由基、超氧阴离子自由基和羟基自由基的IC50值分别为0.53、0.45、0.34 mg/mL。本研究为制备抗氧化肽提供一种新思路。

Abstract:

Three novel polypeptides were designed with trypsin hydrolyzing residues for manufacturing anti-oxidant oligopeptides. These polypeptides successfully expressed in E. coli BL21(DE3) were named as ATO, ATW and WIT, respectively. Three kinds of polypeptide hydrolysates were achieved with trypsin digestion. In vitro antioxidant ability evaluation revealed that the generated polypeptide hydrolysates performed scavenging activity towards different free radicals. In comparison, the ATW hydrolysates showed the highest antioxidant activity, of which the IC50 values of DPPH free radical, superoxide anion free radical and hydroxyl free radical were 0.53 mg/mL, 0.45 mg/mL and 0.34 mg/mL, respectively. The present study provided a novel approach for antioxidant peptides design.