Self‐Assembly of Unprotected Dipeptides into Hydrogels: Water‐Channels Make the Difference
| Autor: | Ottavia Bellotto, Paolo Pengo, Marjetka Podobnik, Matic Kisovec, Silvia Marchesan, Slavko Kralj, Rita De Zorzi, Michele Melchionna |
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| Přispěvatelé: | Bellotto, O., Kralj, S., Melchionna, M., Pengo, P., Kisovec, M., Podobnik, M., De Zorzi, R., Marchesan, S. |
| Rok vydání: | 2021 |
| Předmět: |
D-amino acid
Circular dichroism Supramolecular chemistry chirality Infrared spectroscopy Biochemistry Amphiphile Molecular Biology D-amino acids hydrogels peptides self-assembly Rheometry Chemistry Organic Chemistry Water Hydrogels Stereoisomerism Dipeptides peptide Chemical engineering Attenuated total reflection Self-healing hydrogels Molecular Medicine Self-assembly hydrogel |
| Zdroj: | ChemBioChem. 23 |
| ISSN: | 1439-7633 1439-4227 |
| Popis: | Unprotected dipeptides are attractive building blocks for environmentally friendly hydrogel biomaterials by virtue of their low-cost and ease of preparation. This work investigates the self-assembling behaviour of the distinct stereoisomers of Ile-Phe and Phe-Ile in phosphate buffered saline (PBS) to form hydrogels, using transmission electron microscopy (TEM), attenuated total reflectance infrared spectroscopy (ATR-IR), circular dichroism (CD), and oscillatory rheometry. Each peptide purity and identity was also confirmed by 1 H- and 13 C-NMR spectroscopy and HPLC-MS. Finally, single-crystal XRD data allowed the key interactions responsible for the supramolecular packing into amphipathic layers or water-channels to be revealed. The presence of the latter in the crystal structure is a distinctive feature of the only gelator of this work that self-organizes into stable hydrogels, with fast kinetics and the highest elastic modulus amongst its structural isomers and stereoisomers. |
| Databáze: | OpenAIRE |
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