Valero M L, Camarero J A, Adeva A, Verdaguer N, Fita I, Mateu M G, Domingo E, Giralt E, Andreu D
Department of Organic Chemistry, University of Barcelona, Spain.
Biomed Pept Proteins Nucleic Acids. 1995;1(3):133-40.
Conformationally restricted cyclic peptide mimics of the antigenic site A of foot-and-mouth disease virus serotype C-S8c1 have been designed, first by comparison to the three-dimensional structure of the O1BFS serotype, later more accurately on the basis of X-ray diffraction data from a complex between a linear peptide reproducing site A and an FMDV-derived monoclonal antibody Fab fragment. A variety of cyclization strategies have been attempted, both in solution and in the solid phase, involving disulfide, side chain lactam and head-to-tail arrangements. Preliminary immunological results have shown one of the cyclic disulfide mimics to be a better immunogen than its linear counterpart.
通过与O1BFS血清型的三维结构进行比较,首先设计了C-S8c1型口蹄疫病毒抗原位点A的构象受限环肽模拟物,随后根据来自线性肽再现位点A与口蹄疫病毒衍生的单克隆抗体Fab片段之间复合物的X射线衍射数据进行了更精确的设计。已经尝试了多种环化策略,包括溶液和固相中的二硫键、侧链内酰胺和头尾排列。初步免疫学结果表明,其中一种环二硫键模拟物比其线性对应物是更好的免疫原。