Solution structure of the anticancer p28 peptide in biomimetic medium.
NMR spectroscopy
anticancer peptide
p28
p53 protein
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
Nov 2021
Nov 2021
Historique:
revised:
20
05
2021
received:
25
03
2021
accepted:
31
05
2021
pubmed:
22
6
2021
medline:
14
1
2022
entrez:
21
6
2021
Statut:
ppublish
Résumé
The p28 peptide derived from Pseudomonas aeruginosa azurin shows an anticancer activity after binding to p53 protein and is currently in Phase I of clinical trials. We have studied its structure in water and in a biomimetic media and show that the peptide is unstructured in water but when studied in a biomimetic medium assumes a structure very similar to the one observed in azurin, suggesting a high propensity of this peptide to maintain this secondary structure. Analysis of p28 sequences from different bacterial species indicates conservation of the secondary structure despite amino acid replacement in different positions, suggesting that others, similar peptides could be tested for binding to p53.
Substances chimiques
Antineoplastic Agents
0
Peptide Fragments
0
Peptides
0
Azurin
12284-43-4
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3357Subventions
Organisme : Fondazione Cassa di Risparmio di Firenze
ID : Dalla struttura tridimensionale di antigeni protei
Organisme : iNEXT, funded by the Horizon 2020 programme of the European Union
ID : Project number 653706
Informations de copyright
© 2021 European Peptide Society and John Wiley & Sons, Ltd.
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