Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers
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 he...
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| Veröffentlicht in: | Analytica chimica acta 2017-04, Vol.960, p.131-137 |
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| container_title | Analytica chimica acta |
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| creator | Olajos, Gábor Bartus, Éva Schuster, Ildikó Lautner, Gergely Gyurcsányi, Róbert E. Szögi, Titanilla Fülöp, Lívia Martinek, Tamás A. |
| description | 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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•A sandwich-type immunoassay is developed to detect β-amyloid.•The assay utilizes foldamer helices as recognition elements.•The assay is selective to β-amyloid oligomers against monomeric forms.•β-amyloid oligomers can be detected at pM levels. |
| doi_str_mv | 10.1016/j.aca.2017.01.013 |
| format | Article |
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[Display omitted]
•A sandwich-type immunoassay is developed to detect β-amyloid.•The assay utilizes foldamer helices as recognition elements.•The assay is selective to β-amyloid oligomers against monomeric forms.•β-amyloid oligomers can be detected at pM levels.</description><identifier>ISSN: 0003-2670</identifier><identifier>EISSN: 1873-4324</identifier><identifier>DOI: 10.1016/j.aca.2017.01.013</identifier><identifier>PMID: 28193356</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Amyloid beta-Peptides - chemistry ; Antibody mimetics ; Bioaffinity assay ; Enzyme-Linked Immunosorbent Assay - methods ; Foldamers ; Models, Molecular ; Molecular recognition ; Protein Aggregates ; Protein Conformation, alpha-Helical ; Protein Multimerization ; Protein Structure, Secondary ; Time Factors ; β-Amyloid oligomers</subject><ispartof>Analytica chimica acta, 2017-04, Vol.960, p.131-137</ispartof><rights>2017 Elsevier B.V.</rights><rights>Copyright © 2017 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c396t-b9f7e371867f984c52ff0a3ecd556a20a84679454ee06ba472e1fbc4c7e3abec3</citedby><cites>FETCH-LOGICAL-c396t-b9f7e371867f984c52ff0a3ecd556a20a84679454ee06ba472e1fbc4c7e3abec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003267017300922$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28193356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Olajos, Gábor</creatorcontrib><creatorcontrib>Bartus, Éva</creatorcontrib><creatorcontrib>Schuster, Ildikó</creatorcontrib><creatorcontrib>Lautner, Gergely</creatorcontrib><creatorcontrib>Gyurcsányi, Róbert E.</creatorcontrib><creatorcontrib>Szögi, Titanilla</creatorcontrib><creatorcontrib>Fülöp, Lívia</creatorcontrib><creatorcontrib>Martinek, Tamás A.</creatorcontrib><title>Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers</title><title>Analytica chimica acta</title><addtitle>Anal Chim Acta</addtitle><description>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.
[Display omitted]
•A sandwich-type immunoassay is developed to detect β-amyloid.•The assay utilizes foldamer helices as recognition elements.•The assay is selective to β-amyloid oligomers against monomeric forms.•β-amyloid oligomers can be detected at pM levels.</description><subject>Amino Acid Sequence</subject><subject>Amyloid beta-Peptides - chemistry</subject><subject>Antibody mimetics</subject><subject>Bioaffinity assay</subject><subject>Enzyme-Linked Immunosorbent Assay - methods</subject><subject>Foldamers</subject><subject>Models, Molecular</subject><subject>Molecular recognition</subject><subject>Protein Aggregates</subject><subject>Protein Conformation, alpha-Helical</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Secondary</subject><subject>Time Factors</subject><subject>β-Amyloid oligomers</subject><issn>0003-2670</issn><issn>1873-4324</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1LwzAUhoMobk5_gDfSS29a89W0xasx_IKJN_M6pOnJyGibmbSD_S1_iL_JjKmXwoEQzvO-cB6ErgnOCCbibpMprTKKSZFhEoedoCkpC5ZyRvkpmmKMWUpFgSfoIoRN_FKC-Tma0JJUjOViilavYzvYnWqhHxLj2kZ14NNaBWgSZYzt7bBPVAhqH7c-CdCCjjwkHrRbx611feJMMv_6TFxr1y7GwyU6M6oNcPXzztD748Nq8Zwu355eFvNlqlklhrSuTAGsIKUoTFVynVNjsGKgmzwXimJVclFUPOcAWNSKFxSIqTXXMaVq0GyGbo-9W-8-RgiD7GzQ0LaqBzcGGZtLVuWckYiSI6q9C8GDkVtvO-X3kmB5kCk3MsqUB5kSkzgsZm5-6se6g-Yv8WsvAvdHAOKROwteBm2h19DYqGeQjbP_1H8D2O2GaA</recordid><startdate>20170401</startdate><enddate>20170401</enddate><creator>Olajos, Gábor</creator><creator>Bartus, Éva</creator><creator>Schuster, Ildikó</creator><creator>Lautner, Gergely</creator><creator>Gyurcsányi, Róbert E.</creator><creator>Szögi, Titanilla</creator><creator>Fülöp, Lívia</creator><creator>Martinek, Tamás A.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20170401</creationdate><title>Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers</title><author>Olajos, Gábor ; Bartus, Éva ; Schuster, Ildikó ; Lautner, Gergely ; Gyurcsányi, Róbert E. ; Szögi, Titanilla ; Fülöp, Lívia ; Martinek, Tamás A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c396t-b9f7e371867f984c52ff0a3ecd556a20a84679454ee06ba472e1fbc4c7e3abec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Amino Acid Sequence</topic><topic>Amyloid beta-Peptides - chemistry</topic><topic>Antibody mimetics</topic><topic>Bioaffinity assay</topic><topic>Enzyme-Linked Immunosorbent Assay - methods</topic><topic>Foldamers</topic><topic>Models, Molecular</topic><topic>Molecular recognition</topic><topic>Protein Aggregates</topic><topic>Protein Conformation, alpha-Helical</topic><topic>Protein Multimerization</topic><topic>Protein Structure, Secondary</topic><topic>Time Factors</topic><topic>β-Amyloid oligomers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Olajos, Gábor</creatorcontrib><creatorcontrib>Bartus, Éva</creatorcontrib><creatorcontrib>Schuster, Ildikó</creatorcontrib><creatorcontrib>Lautner, Gergely</creatorcontrib><creatorcontrib>Gyurcsányi, Róbert E.</creatorcontrib><creatorcontrib>Szögi, Titanilla</creatorcontrib><creatorcontrib>Fülöp, Lívia</creatorcontrib><creatorcontrib>Martinek, Tamás A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Analytica chimica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Olajos, Gábor</au><au>Bartus, Éva</au><au>Schuster, Ildikó</au><au>Lautner, Gergely</au><au>Gyurcsányi, Róbert E.</au><au>Szögi, Titanilla</au><au>Fülöp, Lívia</au><au>Martinek, Tamás A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers</atitle><jtitle>Analytica chimica acta</jtitle><addtitle>Anal Chim Acta</addtitle><date>2017-04-01</date><risdate>2017</risdate><volume>960</volume><spage>131</spage><epage>137</epage><pages>131-137</pages><issn>0003-2670</issn><eissn>1873-4324</eissn><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.
[Display omitted]
•A sandwich-type immunoassay is developed to detect β-amyloid.•The assay utilizes foldamer helices as recognition elements.•The assay is selective to β-amyloid oligomers against monomeric forms.•β-amyloid oligomers can be detected at pM levels.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>28193356</pmid><doi>10.1016/j.aca.2017.01.013</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Amyloid beta-Peptides - chemistry Antibody mimetics Bioaffinity assay Enzyme-Linked Immunosorbent Assay - methods Foldamers Models, Molecular Molecular recognition Protein Aggregates Protein Conformation, alpha-Helical Protein Multimerization Protein Structure, Secondary Time Factors β-Amyloid oligomers |
| title | Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers |
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