Tuning the elastic modulus of hydrated collagen fibrils.

Systematic variation of solution conditions reveals that the elastic modulus (E) of individual collagen fibrils can be varied over a range of 2-200 MPa. Nanoindentation of reconstituted bovine Achilles tendon fibrils by atomic force microscopy (AFM) under different aqueous and ethanol environments was carried out. Titration of monovalent salts up to a concentration of 1 M at pH 7 causes E to increase from 2 to 5 MPa. This stiffening effect is more pronounced at lower pH where, at pH 5, e.g., there is an approximately 7-fold increase in modulus on addition of 1 M KCl. An even larger increase in modulus, up to approximately 200 MPa, can be achieved by using increasing concentrations of ethanol. Taken together, these results indicate that there are a number of intermolecular forces between tropocollagen monomers that govern the elastic response. These include hydration forces and hydrogen bonding, ion pairs, and possibly the hydrophobic effect. Tuning of the relative strengths of these forces allows rational tuning of the elastic modulus of the fibrils.