Self-Assembling Peptide of d-Amino Acids Boosts Selectivity and Antitumor Efficacy of 10-Hydroxycamptothecin
Citations Over TimeTop 10% of 2014 papers
Abstract
D-peptides, which consist of D-amino acids and can resist the hydrolysis catalyzed by endogenous peptidases, are one of the promising candidates for construction of peptide materials with enhanced biostability in vivo. In this paper, we report on a self-assembling supramolecular nanostructure of D-amino acid-based peptide Nap-G(D)F(D)F(D)YGRGD (D-fiber, (D)F meant D-phenylalanine, (D)Y meant D-tyrosine), which were used as carriers for 10-hydroxycamptothecin (HCPT). Transmission electron microscopy observations demonstrated the filamentous morphology of the HCPT-loaded peptides (d-fiber-HCPT). The better selectivity and antitumor activity of D-fiber-HCPT than L-fiber-HCPT were found in the in vitro and in vivo antitumor studies. These results highlight that this model D-fiber system holds great promise as vehicles of hydrophobic drugs for cancer therapy.
Related Papers
- → Oligothiophene Versus β‐Sheet Peptide: Synthesis and Self‐Assembly of an Organic Semiconductor‐Peptide Hybrid(2009)127 cited
- → Self-Assembling Peptide-Polymer Hydrogels Designed From the Coiled Coil Region of Fibrin(2008)110 cited
- → Mechanical characteristics of beta sheet-forming peptide hydrogels are dependent on peptide sequence, concentration and buffer composition(2018)49 cited
- → Insight into the self-assembly and gel formation of a bioactive peptide derived from bovine casein(2023)14 cited
- IKVAV-containing Peptide self-assembly into Hydrogel(2008)