| dc.description.abstract | Self-assembly is the spontaneous aggregation process which disordered molecules organize into ordered or functional structures through specific interactions, which is a common
way of building nanostructures. In life science, self-assembly processes are widely identified in cell biology, including the formations of phospholipid membrane, protein superstructure, DNA quadruplex and other molecules. Among them, some amphiphilic materials form three-dimensional interconnected network structure. This network structure in an aqueous environment will absorb water to form hydrogel at the macroscopic level. Common hydrogel-forming materials can be divided into two categories including synthetic materials [e.g., poly(acrylic acid) and polyethylene glycol] and natural ones (e.g., hyaluronic acid and peptide). Synthetic materials have strong mechanical properties and easy to modify through the change of monomers. On the other hand, natural materials benefit from their superior biocompatibility and biodegradability. Among these cases, peptide-based hydrogel possesses the advantage of both cases. They are biocompatible and easy to modify through the change of sequence or amino acid modification. In this study, we designed a series of chemically-engineer peptides for preparing hydrogel. We observed that some peptides self-assembled into spherical-like structures in acid or neutral conditions but transformed into hydrogel with nano-fibrils in base conditions. We also found that high peptide concentration and the addition of hydrophobic amino acids could promote gel formation. Moreover, increasing the hydrophobicity makes the peptide able to form hydrogel in neutral condition. Finally, we successfully seeded L929 fibroblast cells onto the hydrogel at neutral pH value,
indicating this chemically-engineered peptides could be applied as a biocompatible material. | en_US |