Journal Article

FZJ-2019-04002

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Solution-Based Determination of Dissociation Constants for the Binding of Aβ42 to Antibodies

Zhang, T.FZJ* ; Nagel-Steger, L. (Corresponding author)FZJ* ; Willbold, D.FZJ*

2019
Wiley-VCH-Verl. Weinheim

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Please use a persistent id in citations: http://hdl.handle.net/2128/22715  doi:10.1002/open.201900167

Abstract: Amyloid β‐peptides (Aβ) play a major role in the pathogenesis of Alzheimer's disease. Therefore, numerous monoclonal antibodies against Aβ have been developed for basic and clinical research. The present study applied fluorescence based analytical ultracentrifugation and microscale thermophoresis to characterize the interaction between Aβ42 monomers and three popular, commercially available antibodies, namely 6E10, 4G8 and 12F4. Both methods allowed us to analyze the interactions at low nanomolar concentrations of analytes close to their dissociation constants (KD) as required for the study of high affinity interactions. Furthermore, the low concentrations minimized the unwanted self‐aggregation of Aβ. Our study demonstrates that all three antibodies bind to Aβ42 monomers with comparable affinities in the low nanomolar range. KD values for Aβ42 binding to 6E10 and 4G8 are in good agreement with formerly reported values from SPR studies, while the KD for 12F4 binding to Aβ42 monomer is reported for the first time.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 553 - Physical Basis of Diseases (POF3-553) (POF3-553)

Appears in the scientific report 2019

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Database coverage:
; ; ; ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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