Hydrogels from the assembly of SAA/elastin-inspired peptides reveal non-canonical nanotopologies

Peptide-based hydrogels are of great interest in the biomedical field, according to their biocompatibility, simple structure, and tunable properties via sequence modification. In recent years multicomponent assembly of peptides has expanded the possibilities to produce more versatile hydrogels, by blending gelating peptides with different types of peptides to add new features. In the present study assembly of gelating P5 peptide, SFFSF, blended with P21 peptide, SFFSFGVPGVGVPGVGSFFSF an elastin-inspired peptides or alternatively with FF dipeptide, was investigated by oscillatory rheology and different microscopy techniques in order to shed light on the nanotopologies formed by the self-assembled peptide mixtures. Our data show that, depending on the added peptides, cooperative or disruptive assembly can be observed giving rise to distinct nanotopologies to which correspond different mechanical properties that could be exploited to fabricate materials of desired properties.