Effect of acetic acid on the adhesion-capillary interaction of an atomic force microscope probe with immunoglobulin G

It is established that the interaction of immunoglobulin G with 1% acetic acid increases the adhesion-capillary interaction between the atomic force microscope probe and immunoglobulin G covalently bound to the surface of the glass more than 2 times. Changes in the Fourier-IR absorption band of the first and second amide bands of immunoglobulin G due to the interaction of protein with 1% acetic acid indicates a change in the secondary structure of protein in favor of the component of β-sheet structure with a peak of 1635 ± 1 cm⁻¹. It is concluded that the probable cause of the change of adhesion-capillary interaction is a change in the secondary structure of proteins.