Amphipathic helical peptides hamper protein-protein interactions of the intrinsically disordered chromatin nuclear protein 1 (NUPR1)

• Published in: Biochimica et biophysica acta. General subjects Vol. 1862; no. 6; pp. 1283 - 1295
• Main Authors: Santofimia-Castaño, Patricia, Rizzuti, Bruno, Abián, Olga, Velázquez-Campoy, Adrián, Iovanna, Juan L., Neira, José L.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2018; Elsevier
• Subjects: adenocarcinoma; Basic Helix-Loop-Helix Transcription Factors - chemistry; Basic Helix-Loop-Helix Transcription Factors - genetics; Basic Helix-Loop-Helix Transcription Factors - metabolism; Calorimetry; Cancer; Capsid Proteins - chemistry; chromatin; circular dichroism spectroscopy; dissociation; Drug design; fluorescence; Humans; Hydrophobic and Hydrophilic Interactions; hydrophobicity; Life Sciences; mice; Molecular dynamics; Molecular Dynamics Simulation; mutants; Mutation; Neoplasm Proteins - chemistry; Neoplasm Proteins - genetics; Neoplasm Proteins - metabolism; NMR; nuclear magnetic resonance spectroscopy; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptides; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; protein-protein interactions; surfactants; titration; trifluoperazine; CD; PLA; Peptides; ANS; PPI; Molecular dynamics; MSL1; NMR; PDAC; IDP; C-RING1B; MD; ITC; Calorimetry; Drug design; NUPR1; SLiM; TFP; Cancer

NUPR1 is a multifunctional intrinsically disordered protein (IDP) involved, among other functions, in chromatin remodelling, and development of pancreatic ductal adenocarcinoma (PDAC). It interacts with several biomolecules through hydrophobic patches around residues Ala33 and Thr68. The drug triflu...