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Wöllner, K. ; Chen, X. ; Kremmer, E. ; Krämer, P.M.

Comparative surface plasmon resonance and enzyme-linked immunosorbent assay characterisation of a monoclonal antibody with N-acyl homoserine lactones.

Anal. Chim. Acta 683, 113-118 (2010)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
This study shows the detection of (N-acyl) homoserine lactones (AHLs or HSL) with monoclonal antibodies via a surface plasmon resonance (SPR)-based immunosensor in comparison to conventional microtiter plate-based enzyme-linked immunosorbent assay (ELISA). An HSL derivative, named HSL2 (Table 1), was attached to bovine serum albumin (BSA) and the conjugate (HSL2-BSA-r2) was either covalently immobilised on the SPR sensor chip surface via free amino groups or via adsorption on the ELISA polystyrene plate surface. With a newly developed rat monoclonal antibody (mAb HSL1/2 2C10), AHLs were detected sensitively in a competitive format with SPR and ELISA. Well comparable experiments between SPR and ELISA could be obtained in buffers. Moreover, the SPR sensor surface with the immobilised conjugate HSL2-BSA-r2 could be regenerated at least 340 times (regeneration cycles) without loss of activity. The measurement time per cycle was approximately 15min. The competitive detection format for SPR and ELISA allowed the detection in the μgL(-1) range.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Surface plasmon resonance; Enzyme-linked immunosorbent assay; N-acyl homoserine lactone; Competitive format; Immunoassay; Monoclonal antibodies
ISSN (print) / ISBN 0003-2670
e-ISSN 1873-4324
Journal Analytica Chimica Acta
Quellenangaben Volume: 683, Issue: 1, Pages: 113-118 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Ecological Chemistry (IOEC)
Institute of Molecular Immunology (IMI)
Research Unit Microbe-Plant Interactions (AMP)