Peptide-based hydrogels are increasingly used in
pharmaceutical and biomedical applications due to their versatility and
biocompatibility. β-Hairpin design enhances β-strand alignment and
fine-tunes hydrogel physicochemical properties. In this study, we
investigate the design of β-hairpin hydrogelators from two P1-based
(H-FQFQFK-NH2) hexamer strands linked by a D-Pro-L-Pro β-turn.
The fluorinated proline surrogate CF3-ΨPro was evaluated for hairpin
stabilization and gel properties. Hydrogels were characterized for
physicochemical, mechanical, and structural properties, and selected
hydrogels were screened in in vitro drug release experiments. Based on
these data, in vivo hydrogel stability experiments were conducted on
hairpin structures P3 (H-FQFQFKpPFQFQFK-NH2) and its fluorinated
analogue P17 (H-FQFQFKp(L-CF3-ΨPro)FQFQFK-NH2), via
subcutaneous injection in mice. P3 and P17 demonstrated enhanced hydrogel lifespan with 70% and 45% of the hydrogel remaining
at the injection site after 11 days, respectively, versus 10% for P1 after 7 days. These findings highlight the advantage of β-hairpin
peptide hydrogels for prolonged drug delivery.
Link to Publisher’s page: Reaching Increased Hydrogel Stability In Vivo through β-Hairpin Peptide-Based Hydrogels - PubMed