Thermal Responses and Cell Adhesive Properties of Glycosylated Jigsaw‐Shaped Self‐Assembling Peptides

ABSTRACT As represented by the posttranslational modifications of proteins, the chemical modifications of side chains of peptide residues enable to regulate their physicochemical properties, conformation, and biological activities. Glycosylation is a main post‐translational modification, which allows for recognition by partner proteins to exert diverse function including increase in the conformational stability. Here, we studied the effects of glucose modification, which is a representative glycosylation sugar chains, to different positions of an amphiphilic peptide having a jigsaw‐shaped hydrophobic part (JigSAP). JigSAP forms a β‐sheet structure to self‐assemble into fibrous objects providing a hydrogel that can be used as a matrix for regenerative medicine. JigSAPs modified with glucose at the N‐terminus and middle portion were synthesized, and both of them self‐assemble in water to form hydrogels. The hydrogel composed of JigSAP containing the glucose group attached to the N‐terminus undergoes a gel‐to‐sol macroscopic phase transition upon heating, accompanied by a conformational change of JigSAP from the β‐sheet to an α‐helix structure. On the other hand, JigSAP with the glucose group in the middle, retained its β‐sheet structure even at high temperatures maintaining the gel state. Both glucose‐modified JigSAP fibers showed cell adhesion activity similar to that of non‐glycosylated JigSAP. This suggests that the glycosylation is effective in regulating the thermal stability of JigSAP fibers while maintaining their extracellular matrix properties depending on the modification site.