Self-assembling peptide hydrogels (SAPHs) represent emerging cell cultures systems in several biomedical applications. The advantages of SAPHs are mainly ascribed to the absence of toxic chemical cross-linkers, the presence of ECM-like fibrillar structures and the possibility to produce hydrogels with a large range of different mechanical properties. We will present a two-component peptide system with tuneable mechanical properties, consisting of a small pentapeptide (SFFSF-NH2 , SA5N) that acts as a gelator and a larger 21-mer peptide (SFFSF-GVPGVGVPGVG-SFFSF, SA21) designed as a physical cross-linker. The hydrogels formed by different mixtures of the two peptides are made up mainly of antiparallel β-sheet nanofibers entangling in an intricate network. The effect of the addition of SA21 on the morphology of the hydrogels was investigated by atomic force microscopy and transmission electron microscopy and correlated to the mechanical properties of the hydrogel. Finally, the biocompatibility of the hydrogels using 2D cell cultures was tested. © 2018 The Authors. journal Of Biomedical Materials Research Part A Published By Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 535-544, 2019.
Keywords: atomic force microscopy; cell culture; elastin sequence; hydrogel; oscillatory rheology; self-assembling peptides.
© 2018 The Authors. Journal of Biomedical Materials Research Part A published by Wiley Periodicals, Inc.