Xie G X, Miyajima A, Yokota T, Arai K, Goldstein A
Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.
Proc Natl Acad Sci U S A. 1990 Apr;87(8):3180-4. doi: 10.1073/pnas.87.8.3180.
We synthesized several chimeric peptides in which the N-terminal nine residues of dynorphin-32, a peptide selective for the kappa opioid receptor, were replaced by opioid peptides selective for other opioid receptor types. Each chimeric peptide retained the high affinity and type selectivity characteristic of its N-terminal sequence. The common C-terminal two-thirds of the chimeric peptides served as an epitope recognized by the same monoclonal antibody. When bound to receptors on a cell surface or membrane preparation, these peptides could still bind specifically to the monoclonal antibody. These chimeric peptides should be useful for isolating mu, delta, and kappa opioid receptors and for identifying opioid receptors on transfected cells in expression cloning procedures. The general approach using chimeric peptides should be applicable to other peptide receptors.
我们合成了几种嵌合肽,其中强啡肽 - 32(一种对κ阿片受体具有选择性的肽)的N端九个残基被对其他阿片受体类型具有选择性的阿片肽所取代。每种嵌合肽都保留了其N端序列的高亲和力和类型选择性特征。嵌合肽共同的C端三分之二作为被同一单克隆抗体识别的表位。当与细胞表面或膜制剂上的受体结合时,这些肽仍能特异性结合单克隆抗体。这些嵌合肽应有助于分离μ、δ和κ阿片受体,并在表达克隆程序中鉴定转染细胞上的阿片受体。使用嵌合肽的一般方法应适用于其他肽受体。