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...
Elmentve itt :
| Szerzők: | |
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2017
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| Sorozat: | ANALYTICA CHIMICA ACTA
960 |
| doi: | 10.1016/j.aca.2017.01.013 |
| mtmt: | 3193785 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/11875 |
| Tartalmi kivonat: | 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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| Terjedelem/Fizikai jellemzők: | 131-137 |
| ISSN: | 0003-2670 |