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

• Published in: Biochimica et biophysica acta. General subjects Vol. 1861; no. 4; pp. 910 - 921
• Main Authors: Signorelli, Sara, Santini, Simona, Yamada, Tohru, Bizzarri, Anna Rita, Beattie, Craig W., Cannistraro, Salvatore
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2017
• Subjects: Amino Acid Sequence; Atomic Force Spectroscopy; binding capacity; Binding Sites - genetics; Cell Line, Tumor; Cell penetrating peptide; Cell-Penetrating Peptides - metabolism; correlation; DNA-binding domains; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; Docking; Humans; Hydrophobic and Hydrophilic Interactions; hydrophobic bonding; hydrophobicity; Microscopy, Atomic Force - methods; Models, Molecular; Molecular Dynamics Simulation; mutants; Mutation - genetics; Mutations; neoplasms; p53; Peptide Fragments - genetics; Peptide Fragments - metabolism; point mutation; Protein Binding - genetics; Protein Structure, Secondary; Raman spectroscopy; surface plasmon resonance; Surface Plasmon Resonance - methods; Tumor Suppressor Protein p53 - genetics; Tumor Suppressor Protein p53 - metabolism; Mutations; Docking; Atomic Force Spectroscopy; Cell penetrating peptide; Raman spectroscopy; p53

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 po...