抗体对人绒毛膜促性腺激素表位（hCGβ66-80）的识别依赖于游离肽中保留的局部结构。
Antibody recognition of a human chorionic gonadotropin epitope (hCGbeta66-80) depends on local structure retained in the free peptide.
机构信息
School of Physics, University of Edinburgh, Mayfield Road, Edinburgh EH9 3JZ, Scotland, United Kingdom.
出版信息
J Biol Chem. 2011 Jul 15;286(28):25016-26. doi: 10.1074/jbc.M111.246637. Epub 2011 May 18.
Abstract
Human chorionic gonadotropin (hCG) is an important biomarker in pregnancy and oncology, where it is routinely detected and quantified by specific immunoassays. Intelligent epitope selection is essential to achieving the required assay performance. We present binding affinity measurements demonstrating that a typical β3-loop-specific monoclonal antibody (8G5) is highly selective in competitive immunoassays and distinguishes between hCGβ(66-80) and the closely related luteinizing hormone (LH) fragment LHβ(86-100), which differ only by a single amino acid residue. A combination of optical spectroscopic measurements and atomistic computer simulations on these free peptides reveals differences in turn type stabilized by specific hydrogen bonding motifs. We propose that these structural differences are the basis for the observed selectivity in the full protein.
摘要
人绒毛膜促性腺激素（hCG）是妊娠和肿瘤学中的重要生物标志物，通常通过特定的免疫分析方法进行检测和定量。智能表位选择对于实现所需的分析性能至关重要。我们提供了结合亲和力测量结果，证明了一种典型的β3 环特异性单克隆抗体（8G5）在竞争性免疫分析中具有高度选择性，并区分了 hCGβ（66-80）和密切相关的促黄体生成素（LH）片段 LHβ（86-100），它们仅相差一个氨基酸残基。对这些游离肽的光学光谱测量和原子级计算机模拟的组合揭示了由特定氢键模式稳定的转角类型的差异。我们提出，这些结构差异是在完整蛋白质中观察到的选择性的基础。
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