Journal
CHEMICAL SCIENCE
Volume 13, Issue 8, Pages 2286-2295Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1sc05424d
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- Department of Science and Technology
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The self-assembly properties of new biocompatible, thermoreversible fluorescent hydrogels composed of amino acid residues have been reported. Different amino acid residues form different aggregated structures, and a significant gel-to-sol transition occurs in the presence of hypochlorite.
The self-assembly properties of new biocompatible, thermoreversible fluorescent hydrogels, composed of amino acid residues, e.g., L-phenylalanine (PyL-PheOx) and L-tyrosine (PyL-TyrOx), have been reported. Spectroscopic investigations indicate that PyL-PheOx forms pi-stacked 'compact' aggregates, while 'loose' aggregates with stronger CT characteristics are observed for PyL-TyrOx. Both the compounds showed the presence of fibrous networks in the self-assembled state. Circular dichroism spectral studies indicate the formation of M-helical and P-helical structures for PyL-PheOx and PyL-TyrOx, respectively. A striking gel-to-sol transition, caused by oxidative decomposition, is explicitly noticed in the presence of hypochlorite. A mechanistic investigation reveals the oxidation of the acyl aroyl hydrazine core of the gelators in the presence of ClO-. In addition to this, change in the fluorescence emission intensity of the hydrogel in the presence of ClO- is utilized for the analysis of commercial bleach samples. Gel-coated paper strips are also developed for the on-site detection of ClO-. Furthermore, the system is utilized for imaging hypochlorite in live mammalian cells.
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