Unbinding process of adsorbed proteins under external stress studied by atomic force microscopy spectroscopy

AUTOR(ES)

Gergely, C.

FONTE

The National Academy of Sciences

RESUMO

We report the study of the dynamics of the unbinding process under a force load f of adsorbed proteins (fibrinogen) on a solid surface (hydrophilic silica) by means of atomic force microscopy spectroscopy. By varying the loading rate rf, defined by f = rf t, t being the time, we find that, as for specific interactions, the mean rupture force increases with rf. This unbinding process is analyzed in the framework of the widely used Bell model. The typical dissociation rate at zero force entering in the model lies between 0.02 and 0.6 s−1. Each measured rupture is characterized by a force f0, which appears to be quantized in integer multiples of 180–200 pN.

Documentos Relacionados

• Direct observation of the anchoring process during the adsorption of fibrinogen on a solid surface by force-spectroscopy mode atomic force microscopy
• Stepwise unfolding of titin under force-clamp atomic force microscopy
• Segmented nanofibers of spider dragline silk: Atomic force microscopy and single-molecule force spectroscopy
• DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy.
• Interactions between synaptic vesicle fusion proteins explored by atomic force microscopy