​Ultrasmall natural peptides self-assemble to strong temperature-resistant helical fibers in scaffolds suitable for tissue engineering

A new class of systematically designed ultrasmall (tri- to heptamer) peptides presents the smallest natural, non-aromatic structures that self-assemble in water to hydrogels. The peptide motif consists of an aliphatic amino acid tail of decreasing hydrophobicity capped by a polar head. The fibrous scaffolds assemble from nanostructured aggregates to condensed three-dimensional (3D) meshes, entrapping up to 99.9% water and resembling collagen fibers in the extracellular matrix. The resulting hydrogels are biocompatible, heat resistant up to 90 degrees C and demonstrate tunable, high mechanical strength. Given their facile and cost-effective synthesis, these new materials would be attractive for applications ranging from injectable medical therapies to tissue-engineered scaffolds.

DOI: 10.1016/j.nantod.2011.05.001

Ultrasmall peptides Self-assembly Hydrogels Tissue engineering