Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability
Affinity selection of peptide phage libraries against single-wall carbon nanohorns identifies a peptide aptamer with conformational variability
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DOI：
10.1021/la048968m
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发表时间：
2004-09-28
期刊：
影响因子：
3.9
通讯作者：
Shiba, K
中科院分区：
文献类型：
--
作者：
Kase, D;Kulp, JL;Shiba, K
利用噬菌体肽库对单壁碳纳米角（SWHN）的亲和筛选，鉴定具有构象变异性的肽适体。采用CO2激光烧蚀法在室温下制备了SWHN.在M13噬菌体文库的6轮后，观察到结合与输入噬菌体的比率增加，这表明SWNH结合噬菌体集中在混合物中。结果显示，M13噬菌体展示技术能够鉴定12个氨基酸的pIII尾序列DYFSSPYYEQLF，其表现出对SWNH表面的结合偏好。
The identification of peptide aptamer with conformational variability was described using affinity selection of peptide phage libraries against single-wall carbon nanohorns (SWHN). The SWHNs were prepared by CO 2 laser ablation under an Ar gas atmosphere at room temperature. After six rounds of M13 phage library, an increase in ratio of bound to input phages was observed, which indicated that SWNH-binding phages were concentrated in mixture. The results show that M13 phage display technology enables to identify a 12-amino-acid pIII tail sequence, DYFSSPYYEQLF, which exhibits a binding preference for SWNH surfaces.