Molecular basis for the changes in the assembly structures of bioactive peptides.

Peptide supramolecular assemblies can compete with designed proteins in their capacity to offer useful biological functions and structural diversity to synthetic soft matter. Besides the extensive use of peptidic sequences to mimic the functional domains of large proteins, the ability to program a vast array of structures through changes in sequences via straightforward solid-phase synthesis has led to the use of peptides as self-assembling building blocks. In particular, the combination of bioactive and self-assembling epitopes generates customized nanomaterials for various biomedical applications. This potential is particularly interesting given the possibility of integrating multiple biological functionalities into a supramolecular scaffold of peptides. From structural perspective peptide assemblies can generate filaments, 2D-sheets, spheres, networks, helices and more complex shapes that will no doubt be discovered in the future as we learn to master morphogenesis of peptide assemblies. Here we focus on a peptidic system composed by a short multifunctional peptide linked to a hydrophobic peptide sequence.