Cyclic Cell-Penetrating Peptides with Single Hydrophobic Groups.
cell-penetrating peptides
cyclic peptides
drug delivery
permeability
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
16 08 2019
16 08 2019
Historique:
received:
04
06
2019
pubmed:
13
7
2019
medline:
22
8
2020
entrez:
13
7
2019
Statut:
ppublish
Résumé
A new family of cyclic cell-penetrating peptides (CPPs) has been discovered; they differ from previously reported cyclic CPPs by containing only a single hydrophobic residue. The optimal CPP structure consists of four arginine residues and a hydrophobic residue with a long alkyl chain (e.g., a decyl group) in a cyclohexapeptide ring. The most active member of this family, CPP 17, has an intrinsic cellular entry efficiency similar to that of cyclic CPP12, the most active CPP reported to date. However, CPP 17 is 2.8 times more active than CPP12 under high serum protein concentrations, presumably because of the lower protein binding. CPP 17 enters the cell primarily by direct translocation at a relatively low concentration (≥5 μm).
Identifiants
pubmed: 31298779
doi: 10.1002/cbic.201900370
pmc: PMC6752721
mid: NIHMS1050227
doi:
Substances chimiques
Cell-Penetrating Peptides
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2085-2088Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM122459
Pays : United States
Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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