Screening and Antiviral Analysis of Phages That Display Peptides with an Affinity to Subunit C of Porcine Aminopeptidase
Screening and Antiviral Analysis of Phages That Display Peptides with an Affinity to Subunit C of Porcine Aminopeptidase
复制标题
展示与猪氨肽酶 C 亚基有亲和力的肽的噬菌体的筛选和抗病毒分析
DOI:
10.1089/mab.2013.0038
复制
发表时间:
2013-10-01
影响因子:
--
通讯作者:
Sun, Dongbo
中科院分区:
文献类型:
--
作者:
Guo, Donghua;Zhu, Qinghe;Sun, Dongbo
The purified C subunit of the recombinant porcine aminopeptidase N (rpAPN-C) protein was used as an immobilized target to screen potential ligands against rpAPN-C from a 12-mer phage display random peptide library. After five rounds of biopanning, five phage clones showed specific binding affinities to rpAPN-C. In 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl tetrazolium bromide (MTT) assays, the phage clone PM1, which contained the HDAISWTHYHPW peptide sequence, had a protective effect against TGEV infection in swine testis cells. Therefore, the HDAISWTHYHPW peptide sequence has a potential use as a small molecular therapeutic agent against TGEV infection.