Identification and characterization of peptides that bind human ErbB-2 selected from a bacteriophage display library
Identification and characterization of peptides that bind human ErbB-2 selected from a bacteriophage display library
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DOI：
10.1023/a:1019749504418
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发表时间：
2002-05-01
期刊：
影响因子：
--
通讯作者：
Quinn, TP
中科院分区：
文献类型：
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作者：
Karasseva, NG;Glinsky, VV;Quinn, TP
ErbB-2受体是酪氨酸激酶I型受体家族的成员，与许多人类恶性肿瘤有关。ErbB-2在癌细胞中的过表达及其细胞外可及性使其成为开发肿瘤特异性药物的有吸引力的靶点。在这项研究中，随机肽噬菌体展示技术，以确定结合人ErbB-2的胞外结构域的肽。肽KCCYSL，最常见的亲和力选择的噬菌体群体中，是化学合成的。并以其与ErbB-2的结合活性为特征。合成肽对ErbB-2表现出高度特异性，平衡解离常数为30 μ M。在直接细胞结合测定中显现肽与ErbB-2阳性人乳腺癌和前列腺癌细胞的结合。总之，肽KCCYSL具有开发成靶向过表达ErbB-2受体的恶性细胞的癌症成像或治疗剂的潜力。
The ErbB-2 receptor, a member of the tyrosine kinase type I family of receptors, has been implicated in many human malignancies. The overexpression of ErbB-2 in cancer cells as well as its extracellular accessibility makes it an attractive target for the development of tumor-specific agents. In this study, random peptide bacteriophage display technology was employed to identify peptides that bound the extracellular domain of human ErbB-2. The peptide KCCYSL, most frequently occurring in the affinity-selected phage population, was chemically synthesized. and characterized for its binding activities to ErbB-2. The synthetic peptide exhibited high specificity for ErbB-2 and an equilibrium dissociation constant of 30 muM. Peptide binding to ErbB-2 positive human breast and prostate carcinoma cells was visualized in direct cell binding assays. In conclusion, the peptide KCCYSL has the potential to be developed into a cancer imaging or therapeutic agent targeting malignant cells overexpressing the ErbB-2 receptor.