重组人肿瘤坏死因子α抑制肽-抗炎酸性尾巴融合蛋白的生物学活性检测
중조인종류배사인자α억제태-항염산성미파융합단백적생물학활성검측
Detection of Biological Activity of Recombinant Human Tumor Ne?crosis Factor α Inhibitory Peptide Fused with Anti-Inflammatory Acidic Tail
  • 万方数据
    生物技术通讯 생물기술통신
    LETTERS IN BIOTECHNOLOGY
    2012年 6期 837-839 ,共3页

    王玮%丁红梅%李慧%赵强%李洁%夏伟%苏雪婷%陈颖%黄皑雪%高波%李少华%邵宁生

    왕위%정홍매%리혜%조강%리길%하위%소설정%진영%황애설%고파%리소화%소저생

    人肿瘤坏死因子α%抑制肽%抗炎酸性尾巴%TRX 标签%融合蛋白%细胞毒作用 人腫瘤壞死因子α%抑製肽%抗炎痠性尾巴%TRX 標籤%融閤蛋白%細胞毒作用
    인종류배사인자α%억제태%항염산성미파%TRX 표첨%융합단백%세포독작용
    human tumor necrosis factor α%inhibitory peptide%anti-inflammatory acidic tail%TRX tag%fusion protein%cytotoxic activity
    目的:评价原核表达、纯化的6×His-硫氧还蛋白(TRX)-人肿瘤坏死因子α(TNFα)抑制肽-C 端抗炎酸性尾巴融合蛋白的生物学功能.方法:在大肠杆菌中分别表达带 His 标签的 TRX 对照蛋白及 TRX 蛋白融合的人 TNFα抑制肽-抗炎酸性尾巴融合蛋白,并对2种蛋白进行 N2+金属螯合层析纯化,采用 MTT 法检测纯化后的蛋白及化学合成多肽抑制 TNFα标准品对 L929细胞的细胞毒活性.结果:与对照蛋白相比,融合蛋白人 TNFα抑制肽-C 端抗炎酸性尾巴及合成多肽均能拮抗 TNFα标准品对 L929细胞的细胞毒作用.结论:融合蛋白人 TNFα抑制肽-C 端抗炎酸性尾巴及合成肽均能有效拮抗 TNFα的生物学作用,为今后发展抑制 TNFα为主的抗炎生物药物奠定了基础.
    목적:평개원핵표체、순화적6×His-류양환단백(TRX)-인종류배사인자α(TNFα)억제태-C 단항염산성미파융합단백적생물학공능.방법:재대장간균중분별표체대 His 표첨적 TRX 대조단백급 TRX 단백융합적인 TNFα억제태-항염산성미파융합단백,병대2충단백진행 N2+금속오합층석순화,채용 MTT 법검측순화후적단백급화학합성다태억제 TNFα표준품대 L929세포적세포독활성.결과:여대조단백상비,융합단백인 TNFα억제태-C 단항염산성미파급합성다태균능길항 TNFα표준품대 L929세포적세포독작용.결론:융합단백인 TNFα억제태-C 단항염산성미파급합성태균능유효길항 TNFα적생물학작용,위금후발전억제 TNFα위주적항염생물약물전정료기출.
    Objective: To evaluate the biological activity of the purified recombinant fusion protein of N-termi?nal 6×His tag-TRX fused human tumor necrosis factor α(TNFα) inhibitory peptide with a C terminal anti-inflam?matory acidic tail expressed in Escharia coli. Methods: The 6×His tagged TRX control protein and TRX fused hu?man TNFα inhibitory peptide with an anti-inflamatory acidic peptide tail were expressed in genetically engineered E.coli and then purified by nickel metal chelated affinity chromatography. The biological activity of the purified proteins and the chemically systhesized control peptide in inhibiting TNFα cytotoxic activity on the L929 cells was evaluated by MTT assay. Results: The TRX-human TNFα inhibitory peptide-anti-inflamatory acidic peptide tail fusion protein and the synthesized peptide can antagonize the cytotoxic activity of the TNFα standard on L929 cells. Conclusion: The recombinant fusion protein and the inhibitory peptide can antagonize the bioactivity of TNFα effectively, laiding the foundation for the development of anti-inflammatory biomedicine based on antagonist of TNFα in the future.
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