Bacteriophage display and discovery of peptide leads for drug development

被引:127
作者
Lowman, HB
机构
[1] Department of Protein Engineering, Genentech Inc., South San Francisco, CA 94080
来源
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1997年 / 26卷
关键词
combinatorial library; structural biology; molecular mimicry; mutagenesis; drug design;
D O I
10.1146/annurev.biophys.26.1.401
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phage display makes large-peptide diversity libraries readily attainable for identifying novel peptide ligands for receptors and other protein or non-protein targets. This technology kindles enthusiasm for the idea that large and protein-protein interaction surfaces (epitopes) can be distilled down to small pharmacophores. These may be accessible to organic scaffolding, yielding new orally active drugs that might otherwise have taken greater time and effort to be discovered through chemical-library screening. This review, though not comprehensive with respect to the explosive volume of phage display work over the last few years, focuses on recent developments in phage-displayed peptide technology.
引用
收藏
页码:401 / 424
页数:24
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