Vesicle-like Nanocapsules Formed by Self-Assembly of Peptides with Oligoproline and -Leucine

Since drug carriers are envisaged to be used in a wide variety of situations and environments, nanocarriers with diverse properties, such as biocompatibility, biodegradability, nonimmunogenicity, adequate particle size, robustness, and cell permeability, are required. Here, we report the constructio...

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Détails bibliographiques
Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 40(2024), 24 vom: 18. Juni, Seite 12802-12809
Auteur principal: Okamoto, Yui (Auteur)
Autres auteurs: Higuchi, Masahiro, Matsubara, Shogo
Format: Article en ligne
Langue:English
Publié: 2024
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Nanocapsules Peptides Leucine GMW67QNF9C Proline 9DLQ4CIU6V
Description
Résumé:Since drug carriers are envisaged to be used in a wide variety of situations and environments, nanocarriers with diverse properties, such as biocompatibility, biodegradability, nonimmunogenicity, adequate particle size, robustness, and cell permeability, are required. Here, we report the construction of novel nanocapsules with the above-mentioned features by the self-assembly of peptides composed of oligoproline and oligoleucine (i.e., H-Pro10Leu4-NH2 and H-Pro10Leu6-NH2). The peptides self-organized via hydrogen bonds and hydrophobic interactions between oligoleucine moieties to form vesicle-like nanocapsules with cationic oligoproline exposed on the surface. The guest encapsulation experiments revealed that the nanocapsules were capable of uptake of both water-soluble and insoluble compounds. Furthermore, positively charged and/or oligoproline-based peptides are known to improve cell permeability and cellular uptake, suggesting that the peptide nanocapsules are good candidates for nanocarriers to complement liposomes and polymer micelles
Description:Date Completed 18.06.2024
Date Revised 18.06.2024
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.4c01412