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目的：避免生物素化对志贺毒素Ｂ亚基结构功能和生物学活性的影响，从噬菌体肽库中筛选与志贺毒素Ｂ亚基结合的短肽分子。方法：采用抗体捕获法。结果：经过四轮筛选，ＥＬＩＳＡ结果表明，与ＳｔｘＢ结合的噬菌体得到了有效富集，在８６个随机挑选的克隆中，４９个与ＳｔｘＢ结合，阳性克隆的序列也表现出一定的偏向性，在结构明确的２９个克隆中，有１２个克隆（４１％）所编码的短肽序列完全一致。结论：抗体捕获法是有效的。运用噬菌体表面显示技术筛选目的分子时，对于生物素化或其他固定化策略影响到结构功能和生物学活性的某些配体分子而言，抗体捕获法是一种较好的选择，可能具有广泛的适用性。
OBJECTIVE: To avoid the influence of biotinylation on the structural and biological activities of Shiga toxin B subunit and to screen short peptide molecules binding to Shiga toxin B subunit from the phage peptide library. Methods: Antibody capture method. Results: After four rounds of screening, the results of ELISA showed that phage binding to StxB was effectively enriched. Of the 86 randomly selected clones, 49 were stxB-positive, and the positive clones also showed some bias. Of the 29 well-characterized clones, 12 (41%) had identical short peptide sequences encoded by 12 clones. Conclusion: Antibody capture method is effective. When using phage display technology to screen for molecules of interest, antibody capture is a good choice for some ligand molecules that affect the structural and biological activities of biotinylation or other immobilization strategies and may have broad Applicability.