AC Kelvin Probe Force Microscopy Enables Charge Mapping in Water.

Mapping charged chemical groups at the solid-liquid interface is important in many areas, ranging from colloidal systems to biomolecular interactions. However, classical methods to measure surface charges either lack spatial resolution or─like Kelvin-probe force microscopy (KPFM)─cannot be applied in aqueous solutions because a DC bias voltage is used. Here, we show that using AC Kelvin probe force microscopy (AC-KPFM), in which the DC bias is replaced with an AC voltage of sufficiently high frequency, the surface potential of spatially fixated, charged surface groups can be mapped in aqueous solution.

Mechanical properties of collagen fibrils determined by buckling analysis.

The mechanical properties of biological nanofibers such as collagen fibrils are important in many applications, ranging from tissue-engineering to cancer treatment. However, mechanical testing is not straightforward at the nanometer scale. Here, we use the theory of column-buckling to determine the bending properties of individual collagen fibrils.

Mechanical Strain Alters the Surface Charge of Collagen Fibrils.

Collagen fibrils act like nanoscale cables in the extracellular matrix of vertebrate tissues and provide a scaffold for cells to attach to. However, beyond this mechanical function, the surface charge of collagen fibrils is also likely to play an important role. Here, we show that native, type I collagen fibrils from a mammal tendon exhibit a particular dependence of surface charge on longitudinal strain.

Glycation changes molecular organization and charge distribution in type I collagen fibrils.

Collagen fibrils are central to the molecular organization of the extracellular matrix (ECM) and to defining the cellular microenvironment. Glycation of collagen fibrils is known to impact on cell adhesion and migration in the context of cancer and in model studies, glycation of collagen molecules has been shown to affect the binding of other ECM components to collagen. Here we use TEM to show that ribose-5-phosphate (R5P) glycation of collagen fibrils - potentially important in the microenvironment of actively dividing cells, such as cancer cells - disrupts the longitudinal ordering of the molecules in collagen fibrils and, using KFM and FLiM, that R5P-glycated collagen fibrils have a more negative surface charge than unglycated fibrils.

Stretching Single Collagen Fibrils Reveals Nonlinear Mechanical Behavior.

The mechanical properties of collagen fibrils play an important role in cell-matrix interactions and are a manifestation of their molecular structure. Using a, to our knowledge, novel combination of uniaxial, longitudinal straining and radial nanoindentation, we found that type I collagen fibrils show a pronounced nonlinear behavior in the form of strain stiffening at strains from 0 to 15%, followed by strain softening at strains from 15 to 25%. At the molecular scale, this surprising phenomenon can be explained by the combination of unfolding of disordered domains and breaking of native cross-links at different stages of strain.