1. Self‐Assembly of Unprotected Dipeptides into Hydrogels: Water‐Channels Make the Difference
- Author
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Ottavia Bellotto, Paolo Pengo, Marjetka Podobnik, Matic Kisovec, Silvia Marchesan, Slavko Kralj, Rita De Zorzi, Michele Melchionna, Bellotto, O., Kralj, S., Melchionna, M., Pengo, P., Kisovec, M., Podobnik, M., De Zorzi, R., and Marchesan, S.
- Subjects
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 - Abstract
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.
- Published
- 2021
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