There is an increasing need to develop short self-assembling peptides (SAPs) that can form hydrogels for cell engineering and biomedical applications. In this study, we proposed new short self-assembling peptides with a symmetric structure via a urea bond. (FFiO) 2 and (FFiK) 2 were designed as amphiphilic peptides with a hydrophobic domain inside of zwitterionic hydrophilic ends and a urea bond embedded in the hydrophobic domain. The two peptides were synthesized by a liquid-phase method. The simple structural design of these peptides makes their synthesis on a large scale possible. Both (FFiO) 2 and (FFiK) 2 assembled into β-sheet structure and formed stable hydrogels under physiological pH conditions in a pH-responsive manner. The urea bond was important for the formation of transparent hydrogels. Since (FFiK) 2 exhibited self-assembling properties superior to those of (FFiO) 2 , (FFiK) 2 hydrogels were used as scaffolds for cell culture. (FFiK) 2 hydrogels supported cell proliferation without significant cytotoxicity. Therefore, (FFiK) 2 is a beneficial supramolecular peptide hydrogelator for cell engineering.
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