Hudecz F, Price M R
Research Group of Peptide Chemistry, Hungarian Academy of Science, Eötvös L. University, Budapest.
J Immunol Methods. 1992 Mar 4;147(2):201-10. doi: 10.1016/s0022-1759(12)80009-3.
The peptide C A P D T R P A P G has been linked covalently to defined branched polypeptides with a polylysine backbone and side chains of DL-alanine or D-leucine-DL-alanine oligopeptides. The peptide was coupled via its N terminal cysteine to the side chains of the macromolecular carrier to ensure uniform orientation. The compounds were subjected to compositional analyses to characterise the degrees of substitution and secondary structural studies were performed using circular dichroism spectroscopy. The peptide selected for investigation contains the immunodominant sequence P D T R P A P which is expressed in the protein core of epithelial mucins. It is to this region that many anti-mucin monoclonal antibodies bind (Burchell et al., 1989; Price et al., 1990a,b). With these characterised constructs, it has been possible to evaluate the influence of secondary structure upon the binding of monoclonal antibodies which recognise short linear sequences in the synthetic antigenic peptide. The findings are relevant to the design and construction of synthetic immunogens and vaccines as well as to the production of synthetic analogues of clinically relevant antigens (in this case, epithelial mucins associated with breast and ovarian carcinomas).
肽CAPDTRPAPG已与具有聚赖氨酸主链以及DL-丙氨酸或D-亮氨酸-DL-丙氨酸寡肽侧链的特定支链多肽共价连接。该肽通过其N端半胱氨酸与大分子载体的侧链偶联，以确保统一的方向。对这些化合物进行组成分析以表征取代度，并使用圆二色光谱进行二级结构研究。选择用于研究的肽包含免疫显性序列PDTRPAP，其在上皮粘蛋白的蛋白质核心中表达。许多抗粘蛋白单克隆抗体都结合到这个区域（Burchell等人，1989年；Price等人，1990年a、b）。利用这些已表征的构建体，有可能评估二级结构对识别合成抗原肽中短线性序列的单克隆抗体结合的影响。这些发现与合成免疫原和疫苗的设计与构建以及临床相关抗原（在这种情况下，与乳腺癌和卵巢癌相关的上皮粘蛋白）的合成类似物的生产有关。
