Coassembly Behavior and Rheological Properties of a β-Hairpin Peptide with Dicarboxylates
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 f...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 37(2021), 40 vom: 12. Okt., Seite 11657-11664 |
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| Weitere Verfasser: | , , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2021
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Biocompatible Materials Hydrogels Peptides |
| Zusammenfassung: | 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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| Beschreibung: | Date Completed 21.10.2021 Date Revised 21.10.2021 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.1c01376 |