AI Article Synopsis
- * The study found that fluorinated groups in hydrogel formulations significantly increased stiffness compared to nonfluorinated versions, which could enhance functionality.
- * Additionally, hydrogels containing certain fluorinated peptides showed improved stability in drug release tests, with one formulation retaining over 20% of its structure nine days after injection, as seen through imaging techniques.
Article Abstract
Peptide-based hydrogels are of interest to biomedical applications. Herein, we have explored the introduction of fluorinated amino acids in hydrogelator H-FQFQFK-NH () to design a series of fluorinated peptide hydrogels and evaluate the and properties of the most promising analogues. The impact of fluorinated groups on peptide gelation, secondary structure, and self-assembly processes was assessed. We show that fluorine can significantly improve hydrogel stiffness, compared to the nonfluorinated reference . For (H-FQFQF(-CF)K-NH), (H-FQFQF(F)K-NH), and (H-FQFQM(CF)K-NH), microscopy studies scrutinized fiber morphologies and alignment in the network. release studies of hydrogels loaded with an opioid cargo suggested improved hydrogel stability for and . This improved stability was further validated , notably for , giving the most significant increased gel residence time, with more than 20% of hydrogel still present 9 days post-injection, as monitored by nuclear SPECT-CT imaging.
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| http://dx.doi.org/10.1021/acs.biomac.4c00872 | DOI Listing |
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