Force Spectroscopy by Dynamic Atomic Force Microscopy on Bovine Serum Albumin proteins changing the tip hydrophobicity, with piezoelectric tuning fork self-sensing scanning probe

J. Polesel-Maris (1) , Jérémy Legrand (1) , Thomas Berthelot (2) , Alexandre Garcia (2) , Pascal Viel (2) , Ali Makky (1) , Serge Palacin (2)

1 SPCSI - Service de Physique et de Chimie des Surfaces et Interfaces
2 LCSI - Laboratoire de Chimie des Surfaces et Interfaces

A tuning fork AFM (Atomic Force Microscope) scanning probe has been used to study the chemical grafting between a functionnalized tip and BSA (Bovine Serum Albumin) protein. A nonconventional chemistry based on diazonium salts has been applied to control the hydrophobicity and hydrophilicity of the tip termination, and to graft proteins on surface. Unfolding signatures during the protein stretching have been observed, using amplitude modulation (AM-AFM) control of the probe. We propose a methodology to obtain quantitative information of the withdrawal forces from the amplitude and phase signals. Our results demonstrate the great potential of this new piezoelectric probe combined in term of sensitivity and versatility of the chemical functionalization of the tip to analyze biological materials

Domains: Material chemistry

J. Polesel-Maris, Jérémy Legrand, Thomas Berthelot, Alexandre Garcia, Pascal Viel, et al.. Force Spectroscopy by Dynamic Atomic Force Microscopy on Bovine Serum Albumin proteins changing the tip hydrophobicity, with piezoelectric tuning fork self-sensing scanning probe. Sensors and Actuators B: Chemical, 2012, 161, pp.775-783. ⟨10.1016/j.snb.2011.11.032⟩. ⟨cea-00960500⟩