relation: http://publicatio.bibl.u-szeged.hu/11875/
title: Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers
creator:  Olajos Gábor
creator:  Bartus Éva
creator:  Schuster Ildikó
creator:  Lautner Gergely
creator:  Gyurcsányi Ervin Róbert
creator:  Szögi Titanilla
creator:  Fülöp Lívia
creator:  Martinek Tamás A.
description: 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.
date: 2017
type: Folyóiratcikk
type: PeerReviewed
format: text
identifier: http://publicatio.bibl.u-szeged.hu/11875/1/1_s2.0_S0003267017300922_main_u.pdf
identifier:     Olajos Gábor;  Bartus Éva;  Schuster Ildikó;  Lautner Gergely;  Gyurcsányi Ervin Róbert;  Szögi Titanilla;  Fülöp Lívia;  Martinek Tamás A.: Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers.   ANALYTICA CHIMICA ACTA, 960.  pp. 131-137.  ISSN 0003-2670 (2017)     
identifier: doi:10.1016/j.aca.2017.01.013
relation: 3193785
language: eng