Abstract
The effects of changes in the loading rate during the forced dissociation of single bonds have been studied for a wide variety of interactions. Less is known on the loading rate dependent behaviour of more complex systems that consist of multiple bonds. Here we focus on viral nanoparticles, in particular the protein shell (capsid) that protects the viral genome. As model systems we use the well-studied capsids of the plant virus Cowpea Chlorotic Mottle Virus (CCMV) and of the bacteriophages φ29 and HK97. By applying an atomic force microscopy (AFM) nanoindentation approach we study the loading rate dependency of their mechanical properties. Our AFM results show very diverse behaviour for the different systems. In particular, we find that not only the breaking force, but also the spring constant of some capsids depend on the loading rate. We describe and compare the measured data with simulation results from the literature. The unexpected complex loading rate dependencies that we report present a challenge for the current theoretical considerations aimed at understanding the molecular level interactions of highly ordered protein assemblies.
Original language | English |
---|---|
Pages (from-to) | 1343-1350 |
Number of pages | 8 |
Journal | Micron |
Volume | 43 |
Issue number | 12 |
DOIs | |
Publication status | Published - 1 Dec 2012 |
Externally published | Yes |
Funding
We thank Ilya Gertsman and Jack Johnson (Scripps Research Institute, La Jolla, CA, USA), Melanie Brasch and Jeroen Cornelissen (Technische Universiteit Twente, Netherlands) and Xabier Agirrezabala, Roberto Miranda and José Carrascosa (Centro Nacional de Biotecnología of the Consejo Superior de Investigaciones Científicas, Madrid, Spain) for protein preparation. GJLW is supported by a STW-administered NanoSci E+ grant, a VICI grant from the Nederlandse organisatie voor Wetenschappelijk Onderzoek (NWO) and by Fundamenteel Onderzoek der Materie (FOM) through the “Physics of the genome” programme.
Keywords
- Atomic force microscopy
- Dynamic force spectroscopy
- Loading rate
- Macromolecular assemblies
- Nanoindentation
- Virus