Effect of chemical cross-linking on the mechanical properties of elastomeric peptides studied by single molecule force spectroscopy.

Mechanical properties of animal tissues are mainly provided by the assembly of single elastomeric proteins into a complex network of filaments. Even if the overall elastic properties of such a reticulated structure depend on the mechanical characteristics of the constituents, it is not the only aspect to be considered. In addition, the aggregation mechanism has to be clarified to attain a full knowledge of the molecular basis of the elastic properties of natural nanostructured materials. This aim is even more crucial in the process of rational design of biomaterials with selected mechanical properties, in which not only the mechanics of single molecules but also of their assemblies has to be cared of. In this study, this aspect was approached by means of single molecule stretching experiments. In particular, the effect of chemical cross-linking on the mechanical properties of a naturally inspired elastomeric peptide was investigated. Accordingly, we observed that, in order to preserve the elastic properties of the single filament, the two strands of the dimer have to interact with each other. The results thus confirm that the influence of the aggregation process on the mechanical properties of a molecular assembly cannot be neglected.