Olajos Gábor, Bartus Éva, Schuster Ildikó, Lautner Gergely, Gyurcsányi Róbert E, Szögi Titanilla, Fülöp Lívia, Martinek Tamás A
Institute of Pharmaceutical Analysis, University of Szeged, Somogyi u. 4, 6720 Szeged, Hungary.
Department of Medical Chemistry, University of Szeged, Dóm tér 8, 6720 Szeged, Hungary.
Anal Chim Acta. 2017 Apr 1;960:131-137. doi: 10.1016/j.aca.2017.01.013. Epub 2017 Jan 24.
Mimicking the molecular recognition functionality of antibodies is a great challenge. Foldamers are attractive candidates because of their relatively small size and designable interaction surface. This paper describes a sandwich type enzyme-linked immunoassay with a tetravalent β-peptide foldamer helix array as capture element and enzyme labeled tracer antibodies. The assay was found to be selective to β-amyloid oligomeric species with surface features transiently present in ongoing aggregation. In optimized conditions, with special emphasis on the foldamer immobilization, a detection limit of 5 pM was achieved with a linear range of 10-500 pM. These results suggest that protein mimetic foldamers can be useful tools in biosensors and affinity assays.
模拟抗体的分子识别功能是一项巨大的挑战。折叠体因其相对较小的尺寸和可设计的相互作用表面而成为有吸引力的候选者。本文描述了一种夹心型酶联免疫分析方法，该方法以四价β-肽折叠体螺旋阵列作为捕获元件，以酶标记的示踪抗体作为检测试剂。该分析方法被发现对β-淀粉样寡聚体具有选择性，这些寡聚体在持续聚集过程中具有短暂存在的表面特征。在优化条件下，特别强调折叠体的固定化，检测限达到5 pM，线性范围为10 - 500 pM。这些结果表明，蛋白质模拟折叠体可成为生物传感器和亲和分析中的有用工具。
