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Combining a hybrid chip and tube microfluidic system with fluorescent molecularly imprinted polymer (MIP) core–shell particles for the derivatisation, extraction, and detection of peptides with N-terminating phosphorylated tyrosine

  • The reliable identification and quantitation of phosphorylated amino acids, peptides and proteins is one of the key challenges in contemporary bioanalytical research, an area of particular interest when attempting to diagnose and treat diseases at an early stage. We have developed a synthetic probe for targeting phosphorylated amino acids, based on core–shell submicron-sized particles consisting of a silica core, coated with a molecularly imprinted polymer (MIP) shell. The MIP layer contains a fluorescent probe crosslinker which binds selectively to phosphorylated tyrosine (pY) moieties with a significant imprinting factor (IF) and responds with a "light-up” fluorescence signal. The bead-based ratiometric detection scheme has been successfully transferred to a microfluidic chip format and its applicability to rapid assays has been exemplarily shown by discriminating a pY-terminating oligopeptide against its nonphosphorylated counterpart. Such miniaturised devices could lead to anThe reliable identification and quantitation of phosphorylated amino acids, peptides and proteins is one of the key challenges in contemporary bioanalytical research, an area of particular interest when attempting to diagnose and treat diseases at an early stage. We have developed a synthetic probe for targeting phosphorylated amino acids, based on core–shell submicron-sized particles consisting of a silica core, coated with a molecularly imprinted polymer (MIP) shell. The MIP layer contains a fluorescent probe crosslinker which binds selectively to phosphorylated tyrosine (pY) moieties with a significant imprinting factor (IF) and responds with a "light-up” fluorescence signal. The bead-based ratiometric detection scheme has been successfully transferred to a microfluidic chip format and its applicability to rapid assays has been exemplarily shown by discriminating a pY-terminating oligopeptide against its nonphosphorylated counterpart. Such miniaturised devices could lead to an automated pY or pY N-terminated peptide measurement system in the future. The setup combines a modular microfluidic system for amino acid derivatisation, extraction (by micropillar co-flow) and selective adsorption and detection with the fluorescent MIP core–shell particle probes. A miniaturised optical assembly for low-light fluorescence measurements was also developed, based on miniaturised opto-electronic parts and optical fibres. The emission from the MIP particles upon binding of pY or pY N-terminated peptides could be monitored in real-time.zeige mehrzeige weniger

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Metadaten
Autor*innen:Samual BurnageORCiD, Jérémy BellORCiD, Wei Wan, Evgeniia KislenkoORCiD, Knut RurackORCiD
Dokumenttyp:Zeitschriftenartikel
Veröffentlichungsform:Verlagsliteratur
Sprache:Englisch
Titel des übergeordneten Werkes (Englisch):Lab on a Chip
Jahr der Erstveröffentlichung:2022
Organisationseinheit der BAM:1 Analytische Chemie; Referenzmaterialien
1 Analytische Chemie; Referenzmaterialien / 1.9 Chemische und optische Sensorik
Veröffentlichende Institution:Bundesanstalt für Materialforschung und -prüfung (BAM)
Verlag:Royal Society of Chemistry
Verlagsort:Cambridge
Jahrgang/Band:23
Ausgabe/Heft:3
Erste Seite:466
Letzte Seite:474
DDC-Klassifikation:Naturwissenschaften und Mathematik / Chemie / Analytische Chemie
Freie Schlagwörter:Core-shell particles; Fluorescence; Microfluidics; Molecularly imprinted polymers; Phosphorylated peptides
Themenfelder/Aktivitätsfelder der BAM:Umwelt
Umwelt / Sensorik
DOI:10.1039/d2lc00955b
URN:urn:nbn:de:kobv:b43-569204
ISSN:1473-0197
Verfügbarkeit des Dokuments:Datei für die Öffentlichkeit verfügbar ("Open Access")
Lizenz (Deutsch):License LogoCreative Commons - CC BY - Namensnennung 4.0 International
Datum der Freischaltung:30.01.2023
Referierte Publikation:Ja
Datum der Eintragung als referierte Publikation:30.01.2023
Paper des Monats:Ja
Schriftenreihen ohne Nummerierung:Wissenschaftliche Artikel der BAM
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