Directed Intermixing in Multicomponent Self-Assembling Biomaterials

The noncovalent coassembly of multiple different peptides can be a useful route for producing multifunctional biomaterials. However, to date, such materials have almost exclusively been :investigated as homogeneous self-assemblies, having functional components uniformly distributed throughout their, supramolecular structures. Here we illustrate control over the intermixing of Multiple different self-assembling peptides, in turn providing a simple but powerful means for modulating these materials mechanical and biological properties. In beta-sheet fibrillizing hydrogels, significant cant increases in stiffening, could be achieved using heterobifunctional cross-linkers by sequestering peptides bearing different reactive groups into distinct populations of fibrils, favoring interfibril cross-linking. Further, by specifying the intermixing of RGD-bearing peptides in 2-D and 3-D self-assemblies, the growth of HUVECs and NIH 3T3 cells could be significantly modulated. This approach may be immediately applicable toward a wide variety of self-assembling systems that form stable supramolecular structures.