Abstract
We previously reported an artificial collagen gel that can be used as a cell-culture substrate by end-to-end cross-linking of collagen-like triple-helical peptides via disulfide bonds. However, the gel had to be formed a priori by polymerizing the peptide in an acidic solution containing dimethyl sulfoxide for several days, which prevented its use as an injectable gel or three-dimensional (3D) scaffold for cell culture. In this study, we developed a collagen-like peptide polymer by incorporating an O–N acyl migration-triggered triple helix formation mechanism into a collagen-like peptide, which formed a gel within 10 min. We demonstrated that the collagen-like peptide polymer can be used as a 3D cell scaffold and that the 3D structure formation of cells can be controlled by collagen-derived bioactive sequences introduced into the peptide sequence.
Highlights
Undergoes a Sol–Gel TransitionCollagen is the main structural protein in the extracellular matrix, and it forms supramolecules, such as fibrillar and reticular structures, in the body
The peptides were cleaved from the resin tected by a trifluoroacetic acid (TFA)-based cocktail, andcocktail, they were by reverseand deprotected by a trifluoroacetic acid (TFA)-based andpurified they were purified phase high-performance liquid chromatography (RP-HPLC)
We investigated whether the collagen-like peptide polymer optimized above could be applied to 3D cell culture and whether it could regulate specific behaviors of cells by the action of collagen-derived bioactive sequences incorporated into the polymer
Summary
Collagen is the main structural protein in the extracellular matrix, and it forms supramolecules, such as fibrillar and reticular structures, in the body. Cell adhesion activity has been introduced into the artificial collagen-like material by incorporating the integrin-binding GFOGER sequence [20]. It is not suitable for practical use because the need for the stepwise reaction of disulfide bond formation results in high synthetic cost. Collagen-like peptides consisting of Pro-Hyp-Gly repeats with Lys and Asp residues in appropriately designed positions form a gel by elongation of the triple helix through sticky-end assembly and further lateral interactions via salt bridges [21,22]. The amino acid sequence can hardly be rearranged, and it is difficult to incorporate bioactive sequences into the peptide sequence We developed another artificial collagen system by end-to-end cross-linking of collagen-like triple-helical peptides [23]. We found that a glycylserine O-acyl isopeptide unit incorporated into a collagen-like peptide sequence prevented triple helix formation under acidic conditions and induced triple helix formation by conversion to the amide form at pH 7.4 [28]
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