NDLI: Dynamic force spectroscopy on the binding of monoclonal antibodies and tau peptides

Content Provider	Royal Society of Chemistry (RSC)
Author	Hoffmann, Ralf Wagner, Carolin Kremer, Friedrich Stangner, Tim Ueberschär, Olaf Gutsche, Christof Singer, David
Copyright Year	2011
Abstract	Optical tweezers-assisted dynamic force spectroscopy (DFS) is employed to investigate specific receptor/ligand interactions on the level of single binding events. Here, the specific binding of two anti-human tau monoclonal antibodies (mAbs), HPT-110 and HPT-104, to synthetic tau-peptides with different phosphorylation patterns is analyzed. The specificity of HPT-110 to the tau-peptide containing a phosphorylation at Ser235 and of HPT-104 to the tau-peptide containing a phosphorylation at Thr231 is confirmed. Additionally, our approach allows for a detailed characterization of the unspecific interactions that are observed between HPT-104 and the peptide phosphorylated only at Ser235 and between HPT-110 and the peptide phosphorylated only at Thr231. By analyzing the measured rupture-force distributions it is possible to separate unspecific from specific interactions. Thereby for the latter characteristic parameters like the lifetime of the bond without force τ0, the characteristic length xts and the free energy of activation ΔG are determined. The results are in accordance with conventional ELISA tests but offer a much more refined insight.
Starting Page	4370
Ending Page	4378
Page Count	9
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	7
Issue Number	9
Journal	Soft Matter
DOI	10.1039/c0sm01414a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Spectroscopy Phosphorylation Ligand Depth-first search Covalent bond Monoclonal antibody Peptide Thermodynamic free energy
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

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