Ge(001) before and after gold evaporation and annealing
Kernel of the 4-probe microscope (left), crushed tip on Si surface (middle), two STM tips over gold structures on Ge(001) surface

Bio-molecular interactions studied with Dynamic Force Spectroscopy

Molecular Interactions between Myeloma Immunoglobulin Light Chains Studied with a Dynamic Force Spectroscopy

Basic intermolecular interactions causing aggregation of the pathological myeloma immunoglobulin light chains accumulated in disordered deposits (Light Chain Deposit Disease, LCDD) and structurally organized amyloid fibrils (Amyloidosis) have been studied by means of a dynamic force spectroscopy. We have applied an atomic force microscopy/spectroscopy (AFM/AFS) technique for both the relevant protein imaging and for the measurement of the intermolecular force versus distance curves as a function of the loading rate. We have found that the rupturing of the native κ - κ free light chain binding requires overcoming two activation barriers. Similarly, unbinding of the κ free light chains reduced by TECEP involves two energy barriers, although the unbinding forces at the high loading rates are considerably enhanced in comparison to the native κ - κ free light chain interactions. Finally, intermolecular interactions between Bence-Jones proteins modified by cysteine, were studied in order to elucidate the risk reducing effect of the thiol compounds on the dialysis-related amyloidosis by selectively inactivating the amyloidogenic precursors.

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