Single Molecule Force Spectroscopy to Compare Natural versus Artificial Antibody-Antigen Interaction.

Single Molecule Force Spectroscopy to Compare Natural versus Artificial Antibody-Antigen Interaction.
复制标题

单分子力光谱比较自然与人工抗体抗原相互作用。

DOI:
10.1002/smll.201604255
复制
发表时间:
2017-05
期刊:
Small (Weinheim an der Bergstrasse, Germany)
影响因子:
--
通讯作者:
Singamaneni S
Singamaneni S
中科院分区:
其他
文献类型:
--
作者:
Wang C;Hu R;Morrissey JJ;Kharasch ED;Singamaneni S

文献摘要

参考文献

被引文献

相似文献

生物识别是各种生物过程的核心,在化学、生物学和医学的几乎所有领域都有许多应用。通过印迹合成聚合物产生的人工抗体被设计成模拟天然抗体的生物识别能力,同时与其天然对应物相比表现出上级热、化学和环境稳定性。人工抗体对其抗原的结合亲和力表征了这些合成纳米构建体的生物识别能力及其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的研究还很缺乏。在这里,使用原子力显微镜为基础的力光谱,我们表明,人工抗体的抗原(血红蛋白)的结合亲和力弱于天然抗体。分子间相互作用的细微差异体现为基于这些识别元件的生物传感器的生物分析参数的显著差异。使用基于原子力显微镜的力光谱,人工抗体与抗原(血红蛋白)的结合亲和力被发现比天然抗体弱。分子间相互作用的细微差异体现为基于这些识别元件的生物传感器的生物分析参数的显著差异。
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 binding affinity of artificial antibody to antigen, especially at the molecular level, is still lacking. Here, using atomic force microscopy-based force spectroscopy, we 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. Using atomic force microscopy-based force spectroscopy, the binding affinity of an artificial antibody to an antigen (hemoglobin) is found to be 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.
DOI: 10.1016/j.polymer.2006.06.002
发表时间: 2006-07-26
期刊: POLYMER
影响因子: 4.6
作者:
Shulha, Hennady;Foo, Cheryl Wong Po;Tsukruk, Vladirnir V.
通讯作者: Tsukruk, Vladirnir V.
DOI: 10.1083/jcb.138.5.1169
发表时间: 1997-09-08
期刊: The Journal of cell biology
影响因子: --
作者:
Alon R;Chen S;Puri KD;Finger EB;Springer TA
通讯作者: Springer TA
DOI: 10.1007/s11481-012-9416-6
发表时间: 2013-03
影响因子: 6.2
作者:
Lv, Zhengjian;Condron, Margaret M.;Teplow, David B.;Lyubchenko, Yuri L.
通讯作者: Lyubchenko, Yuri L.
DOI: 10.1002/adfm.201202370
发表时间: 2013-04-12
影响因子: 19
作者:
Abbas, Abdennour;Tian, Limei;Morrissey, Jeremiah J.;Kharasch, Evan D.;Singamaneni, Srikanth
通讯作者: Singamaneni, Srikanth
DOI: 10.1021/acsnano.5b00136
发表时间: 2015-05-01
期刊: ACS NANO
影响因子: 17.1
作者:
Casalini, Stefano;Dumitru, Andra C.;Biscarini, Fabio
通讯作者: Biscarini, Fabio