噬菌体展示
表位
肽
肽序列
基因组文库
肽库
大肠杆菌
丝状噬菌体
噬菌体
生物
氨基酸
分子生物学
DNA
模拟电影
化学
线性表位
计算生物学
表位定位
抗体
生物化学
噬菌体
遗传学
基因
作者
Jamie K. Scott,George P. Smith
出处
期刊:Science
[American Association for the Advancement of Science]
日期:1990-07-27
卷期号:249 (4967): 386-390
被引量:2086
标识
DOI:10.1126/science.1696028
摘要
Tens of millions of short peptides can be easily surveyed for tight binding to an antibody, receptor or other binding protein using an "epitope library." The library is a vast mixture of filamentous phage clones, each displaying one peptide sequence on the virion surface. The survey is accomplished by using the binding protein to affinity-purify phage that display tight-binding peptides and propagating the purified phage in Escherichia coli. The amino acid sequences of the peptides displayed on the phage are then determined by sequencing the corresponding coding region in the viral DNA's. Potential applications of the epitope library include investigation of the specificity of antibodies and discovery of mimetic drug candidates.
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