Hybrid hydrogels PEG-biconjugated with silylated amyloidogenic peptide.
Hydrogels hybrid-peptide arrangements are a promising alternative for obtaining biocompatible structures at the nanoscopic scale. Several of combinations between different amino acids allows the construction of a vast number of supramolecular architectures with equally diverse physicochemical properties. Therefore, combining hybrid copolymers with biomolecules makes them interest for biomedical and biomaterials applications, such as tissue engineering and drug delivery systems. In this work a new class of hybrid hydrogels was obtained by the sol-gel process, based on a peptide-b-amyloid sequence composed exclusively by arginine, phenylalanine and glycine (Gly [Arg-Phe]4). This sequence wassynthesized and functionalized with alkoxysilanes, obtained by solid-phase strategies. Then, covalently bound to hybrid silylated PEG. 1H NMR, LC/MS and FTIR analysis were used providing synthesized molecules formation. Infrared data has given information of hybrid hydrogels, and also forms type b-sheet structures. Thermal analysis measurement provides us thermal stability of hydrogels, also corroborates with the structural FTIR data about their formation. Mechanical properties results showed elastic behavior, with storage moduli higher than loss moduli and 0,09 PPS sample showed thixotropic properties. SAXS measures provided information about system organization, demonstrating two distinct regimes. Corroborating with SAXS data electron microscopy and atomic force images revealed amorphous and fibrillar regimes depending on the peptide-silane concentration in the hydrogel matriz.