Visualization of a protein-protein interaction at a single-molecule level by atomic force microscopy

Analytical and Bioanalytical Chemistry
Klaus BonazzaGernot Friedbacher

Abstract

Atomic force microscopy is unmatched in terms of high-resolution imaging under ambient conditions. Over the years, substantial progress has been made using this technique to improve our understanding of biological systems on the nanometer scale, such as visualization of single biomolecules. For monitoring also the interaction between biomolecules, in situ high-speed imaging is making enormous progress. Here, we describe an alternative ex situ imaging method where identical molecules are recorded before and after reaction with a binding partner. Relocation of the identical molecules on the mica surface was thereby achieved by using a nanoscale scratch as marker. The method was successfully applied to study the complex formation between von Willebrand factor (VWF) and factor VIII (FVIII), two essential haemostatic components of human blood. FVIII binding was discernible by an appearance of globular domains appended to the N-terminal large globular domains of VWF. The specificity of the approach could be demonstrated by incubating VWF with FVIII in the presence of a high salt buffer which inhibits the interaction between these two proteins. The results obtained indicate that proteins can maintain their reactivity for subsequent in...Continue Reading

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Citations

Aug 11, 2016·Biophysical Journal·Andrew P SpannEric S G Shaqfeh
Nov 11, 2014·Soft Matter·Sean FitzgibbonEric S G Shaqfeh
May 24, 2015·Analytical and Bioanalytical Chemistry·Klaus BonazzaGernot Friedbacher
Dec 18, 2019·Langmuir : the ACS Journal of Surfaces and Colloids·Xue MiCaryn L Heldt
Nov 14, 2021·Analytical and Bioanalytical Chemistry·Maximilian WinzelyGernot Friedbacher

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