Self-Assembling glycopeptide hydrogels for neuronal differentiation

Supramolecular hydrogels generated by unidirectional self-assembly of short biofunctional peptides
mimic the morphological and biochemical features of the extracellular matrix (ECM).1-2 Importantly,
most ECM proteins are glycosylated -the attached glycans can code bioinformation, affect the
conformation of core protein, and modulate cellular response. As an example, in the central nervous
system, heparan sulfate (HS) proteoglycans are present in the ECM, being essential in neurogenesis by
guiding axon growth and synaptogenesis.3 In this context, we designed a minimalistic HS-mimicking
glycopeptide amphiphile, i.e. Fmoc-diphenylalanine-glucosamine-6-sulfate (Fmoc-FF-GlcN6S), that selfassembles into nanofibers (copycatting the ECM) and gels in aqueous media.