Abstract
Hybrid-peptide hydrogel arrangements are a promising alternative to obtaining biocompatible structures at the nanoscopic scale. In this work, a new class of hybrid hydrogels was obtained through the sol-gel process based on the reaction between an amyloid-like octapeptide sequence [RF]4 (where R = arginine and F = phenylalanine) covalently bonded with glycine-linked alkoxysilanes, and hybrid silylated polyethylene glycol (PEG). 1H nuclear magnetic resonance (NMR), liquid chromatography-mass spectrometry (LC-MS), and Fourier transform infrared spectroscopy (FTIR) analyses were used, resulting in synthesized precursor/intermediate molecules. The structure of hybrid hydrogel fibers was studied by atomic force microscopy (AFM) and small-angle X-ray scattering (SAXS), where the existence of two regions in the Guinier plot was observed, one being predominantly formed by polymer while the other one by peptide chains. The rheological measurements showed that viscoelastic parameters depend on both the amount of silane peptide in the hydrogel matrix and increased temperature. Also, the FTIR spectra indicated the coexistence of antiparallel and parallel β-sheet structure patterns into amyloid fibril hydrogels, which can be modulated by peptide-silane coupling in each formulation. The analyzed hydrogels showed thixotropic and shear-thinning rheology at physiological pH, leaving open the opportunity to topical drug delivery system applications in the future.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
