Disulphide Cross‐Linked Ultrashort Peptide Hydrogelator for Water Remediation
A single amino acid in a peptide sequence can play an important role to tune the self‐assembly and hydrogelation behaviour. Here, a C‐terminal cysteine‐containing ultrashort peptide hydrogelator forms hydrogel through non‐covalent and covalent interactions. Interestingly, the hydrogel is insoluble i...
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Veröffentlicht in: | Chemistry : a European journal 2023-07, Vol.29 (37), p.e202300312-n/a |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | A single amino acid in a peptide sequence can play an important role to tune the self‐assembly and hydrogelation behaviour. Here, a C‐terminal cysteine‐containing ultrashort peptide hydrogelator forms hydrogel through non‐covalent and covalent interactions. Interestingly, the hydrogel is insoluble in water and buffer solutions at different pH values (1‐13) and is thixotropic and injectable. In recent years, removing dyes from contaminated water has become a significant concern because of the shortage of freshwater resources. Therefore, the adsorption of dyes through a reliable, straightforward, nontoxic, cheap, and environmentally friendly adsorbent has become a popular topic. Hence, the hydrogelator was exploited to remove organic dyes from wastewater, harnessing its applicability in the gel phase and solid supports (filter paper and cotton).
A cysteine‐containing ultrashort peptide hydrogelator undergoes disulphide bond formation and forms a self‐supporting, thixotropic, insoluble hydrogel via both covalent and non‐covalent interactions. The resultant hydrogelator was exploited to remove toxic organic dyes from contaminated water in the gel phase and solid supports, indicating its potential applicability for water remediation. |
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ISSN: | 0947-6539 1521-3765 |
DOI: | 10.1002/chem.202300312 |