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Updated: Oct 18, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Coassembly Behavior and Rheological Properties of a β-Hairpin Peptide with Dicarboxylates
Yanqing Ge1, Chen Wang1, Weiqiang Zhang1
1State Key Laboratory of Heavy Oil Processing and Centre for Bioengineering & Biotechnology, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao 266580, China.
Abstract:
To understand the molecular interaction mechanism and develop peptide-based hydrogels, a β-hairpin peptide CBHH was used as the model peptide, and its coassembly performance with succinic, malic, and tartaric dicarboxylates has been investigated with circular dichroism spectroscopy (CD) and atomic force microscopy (AFM). The rheological properties and cell culture performance of the coassembled hydrogels have also been assessed. The results showed that the dicarboxylates could induce the folding and self-assembly of the β-hairpin peptide and promote its gelation at low pH. The effects of the dicarboxylates on peptide self-assembly and hydrogel properties were correlated to their hydroxyl group number. The toxicity of the hydrogel has been assessed with NIH-3T3 cells by MTT and Calcein-AM/PI experiments, and it was confirmed that the hydrogel was biocompatible and could be used as cell culture scaffolds. We hope that this study would provide a novel way for biomaterial fabrication in cell and tissue engineering.
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