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Short self‐assembling peptides with a urea bond: A new type of supramolecular peptide hydrogel materials
Author(s) -
Tsutsumi Hiroshi,
Tanaka Kunifumi,
Chia Jyh Yea,
Mihara Hisakazu
Publication year - 2021
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24214
Subject(s) - self healing hydrogels , supramolecular chemistry , amphiphile , peptide , urea , chemistry , self assembly , combinatorial chemistry , biophysics , polymer chemistry , copolymer , organic chemistry , molecule , biochemistry , polymer , biology
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.