Single-molecule nanomechanical spectroscopy shows calcium ions contribute to chain association and structural flexibility of blood clotting factor VIII
Related Experiment Video
Updated: Jan 26, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
Published on: June 3, 2014
Jie Cheng1, Yadi Wang1, Yatao Pan2
1CAS Key Laboratory of Interfacial Physics and Technology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai, 201800, China; ZhangJiang Lab, Shanghai Synchrotron Radiation Facility, Shanghai Advanced Research Institute, Chinese Academy of Sciences, Shanghai, 201210, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Abstract:
Blood coagulation factor VIII (FVIII) can bind calcium ions and ion-protein interactions appear central importance for both their structure and function in coagulation cascade. However, the mechanism and details of how calcium dependent structure change of proteins to fulfill their function remain to be fully defined. In this work, PeakForce Quantitative Nanomechanics (PF-QNM) mode atomic force microscopy (AFM) was used to map the topography and mechanical properties of FVIII with single protein resolution under different calcium concentrations. The obtained nanomechanical spectroscopy showed that calcium ions play dual roles in the chain association and structural flexibility of FVIII. Low concentration of calcium ions prefer to bind isolated chains and increase their mechanical properties, whereas they link the heavy and light chains to keep the protein re-association under higher ions concentration. Our results provide a novel insight into the mechanistic details of the metal ions on the stability and function of blood clotting proteins.
Related Concept Videos
Lewis Structures of Molecular Compounds and Polyatomic Ions
Ions, Molecules, and Compounds
Ions and Ionic Charges
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Electron Transport Chains
The ETC is comprised of...
Factors Affecting Solubility

