The hidden power of a novel collagen octapeptide: Unveiling its antioxidant and cofactors releasing capacity from polyurethane based systems

Abstract

Aromatic antioxidant peptides are attractive biomolecules that can be used to design supramolecular structures useful in various biomedical applications. Collagen-derived peptides proved to be suitable for a wide range of biological applications. Herein, we introduced a novel amphipathic octapeptide as an essential component in hybrid peptide-polyurethane materials. The octapeptide was synthesized by SPPS, followed by mass confirmation using MALDI-ToF mass spectrometry and characterized by nuclear magnetic resonance and fluorescence spectroscopy. The peptide antioxidant capacity was demonstrated through FRAP and DPPH assays. Our data indicate that the presence of peptide slightly slows down the polyurethane ability to form hydrogels at salt concentration higher than 150 mM. Moreover, the gel formed in the presence of octapeptide can release FAD much faster than NADPH. Preferential weak interactions between peptide and polyurethane structures increase FAD releasing capacity. Our findings will pave the way for the development of new biocompatible materials containing an antioxidant peptide and FAD, a cofactor that modulates the antioxidant function of multiple enzymes simultaneously. These controlled-release platforms created by simple mixing may be suitable for injectable formulation.