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Binding of Amphipathic Cell Penetrating Peptide p28 to Wild Type and Mutated p53 as studied by Raman, Atomic Force and Surface Plasmon Resonance spectroscopies.

Biochimica et biophysica acta. General subjects - 1 Apr 2017

Signorelli Sara, Santini Simona, Yamada Tohru, Bizzarri Anna Rita, Beattie Craig W, Cannistraro Salvatore

Abstract excerpt

BACKGROUND: Mutations within the DNA binding domain (DBD) of the tumor suppressor p53 are found in >50% of human cancers and may significantly modify p53 secondary structure impairing its function. p28, an amphipathic cell-penetrating peptide, binds to the DBD through hydrophobic interaction and induces a posttranslational increase in wildtype and mutant p53 restoring functionality. We use mutation analyses to...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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PMID: 28126403
DOI: 10.1016/j.bbagen.2017.01.022

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SPR

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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