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

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 fo...

Teljes leírás

Elmentve itt :
Bibliográfiai részletek
Szerzők: Olajos Gábor
Bartus Éva
Schuster Ildikó
Lautner Gergely
Gyurcsányi Ervin Róbert
Szögi Titanilla
Fülöp Lívia
Martinek Tamás A.
Dokumentumtípus: Cikk
Megjelent: 2017
Sorozat:ANALYTICA CHIMICA ACTA 960
doi:10.1016/j.aca.2017.01.013

mtmt:3193785
Online Access:http://publicatio.bibl.u-szeged.hu/11875
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520 3 |a 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. 
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700 0 1 |a Schuster Ildikó  |e aut 
700 0 1 |a Lautner Gergely  |e aut 
700 0 1 |a Gyurcsányi Ervin Róbert  |e aut 
700 0 1 |a Szögi Titanilla  |e aut 
700 0 1 |a Fülöp Lívia  |e aut 
700 0 1 |a Martinek Tamás A.  |e aut 
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