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Updated: Jan 20, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Triple helix formation of a collagen model peptide induces cell aggregation formation
Kazuki Yoshida1, Edward Vermeersch2, Sandra Van Vlierberghe2
1Division of Applied Chemistry, Graduate School of Engineering, The University of Osaka, 2-1 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Abstract:
Biofabrication refers to the creation of tissues and organs from biological materials such as cells and proteins, and is often applied in transplantation therapy and drug efficacy evaluation. For such a construct to function as a tissue, it is important for individual cells to interact closely with each other, so tailor-made approaches for the fabrication of cell aggregates to facilitate intercellular interactions are needed. Some researchers are using the DNA chain as a crosslinking site to make cell-cell assemblies, but DNA degradation and the potential risk of an immune response are concerns. A collagen triple helix is resistant to most proteases and is expected to function as a suitable cell assembling motif in a cell assembly method. Herein, we reported a thermoresponsive cell assembly method driven by triple-helix formation of a collagen model peptide (CMP). We synthesized a 4-armed poly (ethylene glycol) (PEG) terminally co-modified with (proline-proline-glycine)10 ((PPG)10) and deoxycholic acid (DCA) (4-arm-PEG-DCA/-(PPG)10) and evaluated the characteristics and the cell-assembling property. It was found that 4.3 times more cell aggregates were formed after cooling under conditions with 4-arm-PEG-DCA/-(PPG)10 than without 4-arm-PEG-DCA/-(PPG)10. Accordingly, we developed a thermoresponsive cell assembly method driven by triple-helix formation of CMP. The use of CMP is expected to be applied in a new cell assembling approach.
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