APPL蛋白,包括APPL1和APPL2,是细胞膜与细胞核之间重要的信息传递者,同时也为细胞增殖所必需。在大肠杆菌表达体系中,表达并纯化了人类APPL2蛋白PTB结构域,然后以此为靶标,利用噬菌体展示技术筛选相互作用肽段。经过3轮筛选,随机挑取48个噬菌体单克隆,进行ELISA分析。7肽序列ERLPFFY和YLTSPKH被证明能与PTB结构域特异地结合。对P3-GST的野生型和将每个氨基酸突变为丙氨酸的突变型的ELISA检测,显示每个氨基酸均是结合所必需的。这些对有关APPL2的PTB结构域功能的进一步研究有参考意义。 APPL proteins, including APPL1 and APPL2, are important messengers of cell membranes and nuclei, and are essential for cell proliferation. In E. coli expression system, the human PT2 domain of APPL2 protein was expressed and purified, and then the phage display technology was used to screen the interacting peptides. After 3 rounds of screening, 48 phage monoclonal were randomly picked for ELISA analysis. The peptide sequences ERLPFFY and YLTSPKH proved to specifically bind to the PTB domain. Examination of the wild type of P3-GST and the mutant that mutates each amino acid to alanine showed that each amino acid was required for binding. These further studies on the function of the PTB domain of APPL2 have reference significance.