Geysen H M, Rodda S J, Mason T J
Mol Immunol. 1986 Jul;23(7):709-15. doi: 10.1016/0161-5890(86)90081-7.
A technique was developed for identifying peptides with high affinity for a given antibody. By testing a monoclonal antibody directed against a discontinuous antigenic determinant on foot-and-mouth disease virus, peptides mimicking the determinant were identified even though the tertiary structure of the proteins comprising the virus capsid is unknown. The allowable variations in spacing and stereochemistry of the peptides shown to mimic this epitope suggest protein folding in which amino acid residues from three regions, distant from one another in the primary sequence, are brought into close proximity at this epitope. The technique has potential for identification of peptides which will bind with high affinity to receptors other than antibody molecules.
开发了一种用于鉴定与给定抗体具有高亲和力的肽的技术。通过测试针对口蹄疫病毒上不连续抗原决定簇的单克隆抗体,即使组成病毒衣壳的蛋白质的三级结构未知,也鉴定出了模拟该决定簇的肽。显示模拟该表位的肽在间距和立体化学上的允许变化表明蛋白质折叠,其中在一级序列中彼此远离的三个区域的氨基酸残基在该表位处紧密靠近。该技术具有鉴定与抗体分子以外的受体具有高亲和力结合的肽的潜力。