%V 960
%J ANALYTICA CHIMICA ACTA
%O FELTÖLTŐ: Hetényi Anasztázia - ahetenyi@pharm.u-szeged.hu
%T Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers
%L publicatio11875
%A  Olajos GĂĄbor
%A  Bartus Éva
%A  Schuster IldikĂł
%A  Lautner Gergely
%A  GyurcsĂĄnyi Ervin RĂłbert
%A  SzĂśgi Titanilla
%A  FĂźlĂśp LĂ­via
%A  Martinek TamĂĄs A.
%P 131-137
%X Abstract 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.
%D 2017
%R 3193785
%I szte