Solution structure of the anticancer p28 peptide in biomimetic medium. (20th June 2021)

• Record Type: Journal Article
• Authors: Cantini, Francesca; Gianni', Paola; Savarin, Philippe; Bizzarri, Anna Rita; Sette, Marco
• Is Part Of: Journal of peptide science. Volume 27:Number 11(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-06-20
• Subjects: anticancer peptide -- NMR spectroscopy -- p28 -- p53 protein; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.3357
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : 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. Abstract : Here we solve the solution structure of the anticancer p28 peptide in biomimetic media. The structure is similar to the same region of the native azurin protein. A bioinformatics analysis starting from the p28 amino acid sequence gives us hints as to how potential candidate peptides can be successfully formulated.