Department of Mechanical Engineering and Materials Science, Institute of Materials Science and Engineering, Washington University in St. Louis, Saint Louis, MO, 63130, USA.
Department of Anesthesiology, Washington University in St. Louis, St. Louis, MO, 63110, USA.
Small. 2017 May;13(19). doi: 10.1002/smll.201604255. Epub 2017 Mar 21.
Biorecognition is central to various biological processes and finds numerous applications in virtually all areas of chemistry, biology, and medicine. Artificial antibodies, produced by imprinting synthetic polymers, are designed to mimic the biological recognition capability of natural antibodies, while exhibiting superior thermal, chemical, and environmental stability compared to their natural counterparts. The binding affinity of the artificial antibodies to their antigens characterizes the biorecognition ability of these synthetic nanoconstructs and their ability to replace natural recognition elements. However, a quantitative study of the binding affinity of an artificial antibody to an antigen, especially at the molecular level, is still lacking. In this study, using atomic force microscopy-based force spectroscopy, the authors show that the binding affinity of an artificial antibody to an antigen (hemoglobin) is weaker than that of natural antibody. The fine difference in the molecular interactions manifests into a significant difference in the bioanalytical parameters of biosensors based on these recognition elements.
生物识别是各种生物过程的核心，几乎在化学、生物学和医学的所有领域都有广泛的应用。人工抗体通过印迹合成聚合物来产生，旨在模拟天然抗体的生物识别能力，同时表现出比天然抗体更高的热稳定性、化学稳定性和环境稳定性。人工抗体对其抗原的结合亲和力表征了这些合成纳米结构的生物识别能力，以及它们替代天然识别元件的能力。然而，人工抗体与抗原结合亲和力的定量研究，特别是在分子水平上，仍然缺乏。在这项研究中，作者使用基于原子力显微镜的力谱法表明，人工抗体与抗原（血红蛋白）的结合亲和力比天然抗体弱。分子相互作用的细微差异体现在基于这些识别元件的生物传感器的生物分析参数上的显著差异。
