Blondelle S E, Houghten R A, Pérez-Payá E
Torrey Pines Institute for Molecular Studies, San Diego, CA 92121, USA.
J Mol Recognit. 1996 Mar-Apr;9(2):163-8. doi: 10.1002/(sici)1099-1352(199603)9:2<163::aid-jmr255>3.0.co;2-6.
The identification of peptides that inhibit the biological functions of proteins was used as a means to explore protein/ligand interactions involved in molecular recognition processes. This approach is based on the use of synthetic combinatorial libraries (SCLs) for the rapid identification of individual peptides that block the interaction of proteins with their biological targets. Thus, each peptide mixture of an all-D-amino acid hexapeptide SCL in a positional scanning format was screened for its ability to inhibit the hemolytic activity of melittin, a model self-assembling protein. The potent inhibitory activity of the identified individual peptides suggests that protein-like complexes are able to specifically bind to peptides having an all-D configuration. These results also show that SCLs are useful for the identification of short, non-hydrolysable sequences having potential intracellular inhibitory activities.
鉴定抑制蛋白质生物学功能的肽被用作探索分子识别过程中蛋白质/配体相互作用的一种手段。这种方法基于使用合成组合文库（SCL）来快速鉴定阻断蛋白质与其生物学靶点相互作用的单个肽。因此，对位置扫描形式的全D - 氨基酸六肽SCL的每个肽混合物进行筛选，以检测其抑制蜂毒肽（一种典型的自组装蛋白质）溶血活性的能力。所鉴定的单个肽的强效抑制活性表明，类蛋白质复合物能够特异性结合具有全D构型的肽。这些结果还表明，SCL可用于鉴定具有潜在细胞内抑制活性的短的、不可水解的序列。
