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Probing the physicochemical interactions of 3-hydroxy-benzo[a]pyrene with different monoclonal and recombinant antibodies by use of fluorescence line-narrowing spectroscopy

  • Characterization of interactions between antigens and antibodies is of utmost importance both for fundamental understanding of the binding and for development of advanced clinical diagnostics. Here, fluorescence line-narrowing (FLN) spectroscopy was used to study physicochemical interactions between 3-hydroxybenzo[a]pyrene (3OH-BaP, as antigen) and a variety of solvent matrices (as model systems) or anti-polycyclic aromatic hydrocarbon antibodies (anti-PAH). We focused the studies on the specific physicochemical interactions between 3OH-BaP and different, previously obtained, monoclonal and recombinant anti-PAH antibodies. Control experiments performed with non-binding monoclonal antibodies and bovine serum albumin (BSA) indicated that nonspecific interactions did not affect the FLN spectrum of 3OH-BaP. The spectral positions and relative intensities of the bands in the FLN spectra are highly dependent on the molecular environment of the 3OH-BaP. The FLN bands correlate with different vibrational modes of 3OH-BaP which are affected byCharacterization of interactions between antigens and antibodies is of utmost importance both for fundamental understanding of the binding and for development of advanced clinical diagnostics. Here, fluorescence line-narrowing (FLN) spectroscopy was used to study physicochemical interactions between 3-hydroxybenzo[a]pyrene (3OH-BaP, as antigen) and a variety of solvent matrices (as model systems) or anti-polycyclic aromatic hydrocarbon antibodies (anti-PAH). We focused the studies on the specific physicochemical interactions between 3OH-BaP and different, previously obtained, monoclonal and recombinant anti-PAH antibodies. Control experiments performed with non-binding monoclonal antibodies and bovine serum albumin (BSA) indicated that nonspecific interactions did not affect the FLN spectrum of 3OH-BaP. The spectral positions and relative intensities of the bands in the FLN spectra are highly dependent on the molecular environment of the 3OH-BaP. The FLN bands correlate with different vibrational modes of 3OH-BaP which are affected by interactions with the molecular environment (pi-pi interactions, H-bonding, or van-der-Waals forces). Although the analyte (3OH-BaP) was the same for all the antibodies investigated, different binding interactions could be identified from the FLN spectra on the basis of structural flexibility and conformational multiplicity of the antibodies' paratopes.show moreshow less

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Author details:Ursula EisoldORCiDGND, Annette Kupstat, Dennis Tobias KlierGND, Philipp-A. Primus, Michael Pschenitza, Reinhard Niessner, Dietmar Knopp, Michael Uwe KumkeORCiDGND
DOI:https://doi.org/10.1007/s00216-013-7584-8
ISSN:1618-2642
ISSN:1618-2650
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/24481618
Title of parent work (English):Analytical & bioanalytical chemistry
Publisher:Springer
Place of publishing:Heidelberg
Publication type:Article
Language:English
Year of first publication:2014
Publication year:2014
Release date:2017/03/27
Tag:Antibody; FLNS; Hapten; Paratope; Polycyclic aromatic hydrocarbons
Volume:406
Issue:14
Number of pages:8
First page:3387
Last Page:3394
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
Peer review:Referiert
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