@article{MTMT:3193785,
	title = {Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers},
	url = {https://m2.mtmt.hu/api/publication/3193785},
	author = {Olajos, Gábor and Bartus, Éva and Schuster, Ildikó and Lautner, Gergely and Gyurcsányi, Ervin Róbert and Szögi, Titanilla and Fülöp, Lívia and Martinek, Tamás},
	doi = {10.1016/j.aca.2017.01.013},
	journal-iso = {ANAL CHIM ACTA},
	journal = {ANALYTICA CHIMICA ACTA},
	volume = {960},
	unique-id = {3193785},
	issn = {0003-2670},
	abstract = {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.},
	keywords = {FOLDAMERS; MOLECULAR RECOGNITION; Antibody mimetics; Bioaffinity assay; β-Amyloid oligomers},
	year = {2017},
	eissn = {1873-4324},
	pages = {131-137},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Bartus, Éva/0000-0001-9976-6978; Schuster, Ildikó/0000-0001-9997-5729; Gyurcsányi, Ervin Róbert/0000-0002-9929-7865; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066}
}