Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers

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Bibliographic Details
Main Authors: Olajos Gábor
Bartus Éva
Schuster Ildikó
Lautner Gergely
Gyurcsányi Ervin Róbert
Szögi Titanilla
Fülöp Lívia
Martinek Tamás A.
Format: Article
Published: 2017
Series:ANALYTICA CHIMICA ACTA 960
AAA
Online access:http://publicatio.bibl.u-szeged.hu/11875
DOI:10.1016/j.aca.2017.01.013
MTMT:3193785
Description
Summary: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.
Physical Description:131-137
ISSN:0003-2670