TY  - JOUR
A1  -  Olajos Gábor
A1  -  Bartus Éva
A1  -  Schuster Ildikó
A1  -  Lautner Gergely
A1  -  Gyurcsányi Ervin Róbert
A1  -  Szögi Titanilla
A1  -  Fülöp Lívia
A1  -  Martinek Tamás A.
Y1  - 2017///
AV  - restricted
ID  - publicatio11875
N1  - FELTÖLT?: Hetényi Anasztázia - ahetenyi@pharm.u-szeged.hu
SN  - 0003-2670
EP  - 137
VL  - 960
TI  - Multivalent foldamer-based affinity assay for selective recognition of A? oligomers
JF  - ANALYTICA CHIMICA ACTA
UR  - http://publicatio.bibl.u-szeged.hu/11875/
SP  - 131
N2  - 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 ?-peptide foldamer helix array as capture element and enzyme labeled tracer antibodies. The assay was found to be selective to ?-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.
ER  -