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将人工合成的编码九肽的随机序列ＤＮＡ片段克隆进丝状噬菌体表达载体ｆＵＳＥ５，经多次电击转化和表达，获得肽段与噬菌体ｐⅢ蛋白融合并展示在噬菌体表面的随机序列九肽表位肽库。库容量达１０１０个克隆。以Ⅳ型胶原酶为靶蛋白，采用亲和纯化筛选模式，从中筛选出Ⅳ型胶原酶结合肽。进一步ＥＬＩＳＡ检测筛选出与Ⅳ型胶原酶特异结合的２０个阳性克隆。序列分析发现一组肽含有ＷＤＸＸＤ的共同序列，一组含有ＷＶＧＸＸＲ的共同序列。其中ＷＤＸＸＤ的序列与Ⅳ型胶原酶单链抗体可变区序列同源。结果表明，多肽库是筛选蛋白特异结合肽的有力工具，表位九肽库的构建和筛选方法的建立为进一步应用筛选具有高亲和力的特异结合肽奠定了基础。
The artificial DNA fragment encoding the nonapeptide was cloned into the filamentous bacteriophage expression vector fUSE5 and transformed into the phage expression vector fUSE5. After several times of electroporation, the fragment was fused with the phage pIII protein and displayed on the surface of the phage. Library. Library capacity of 1010 clones. Using type Ⅳ collagenase as target protein, type Ⅳ collagenase-binding peptide was screened out by affinity purification. Twenty positive clones that specifically bound to type IV collagenase were screened by ELISA. Sequence analysis revealed that a group of peptides contained a common sequence of WDXXD, a set of common sequences containing WVGXXR. The sequence of WDXXD is homologous to the variable region of type IV collagenase single chain antibody. The results showed that the polypeptide library was a powerful tool for screening protein-specific binding peptides. The construction of the epitope library and the establishment of screening methods laid the foundation for the further screening of specific binding peptides with high affinity.