In silico analysis prediction of HepTH1-5 as a potential therapeutic agent by targeting tumour suppressor protein networks.

Item request has been placed! ×
Item request cannot be made. ×
loading   Processing Request
Read More Add to Saved list
  • Additional Information
    • Source:
      Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE
    • Publication Information:
      Publication: June 2012- : Oxon, UK : Taylor & Francis
      Original Publication: Guilderland, NY : Adenine Press, [c1983-
    • Subject Terms:
      Tumor Suppressor Protein p53*/genetics ; Carcinoma, Hepatocellular*; Humans ; Hepcidins ; Molecular Docking Simulation ; Tumor Suppressor Proteins/genetics
    • Abstract:
      Many studies reported that the activation of tumour suppressor protein, p53 induced the human hepcidin expression. However, its expression decreased when p53 was silenced in human hepatoma cells. Contrary to Tilapia hepcidin TH1-5, HepTH1-5 was previously reported to trigger the p53 activation through the molecular docking approach. The INhibitor of Growth (ING) family members are also shown to directly interact with p53 and promote cell cycle arrest, senescence, apoptosis and participate in DNA replication and DNA damage responses to suppress the tumour initiation and progression. However, the interrelation between INGs and HepTH1-5 remains unknown. Therefore, this study aims to identify the mechanism and their protein interactions using in silico approaches. The finding revealed that HepTH1-5 and its ligands had interacted mostly on hotspot residues of ING proteins which involved in histone modifications via acetylation, phosphorylation, and methylation. This proves that HepTH1-5 might implicate in an apoptosis signalling pathway and preserve the protein structure and function of INGs by reducing the perturbation of histone binding upon oxidative stress response. This study would provide theoretical guidance for the design and experimental studies to decipher the role of HepTH1-5 as a potential therapeutic agent for cancer therapy. Communicated by Ramaswamy H. Sarma.
    • Contributed Indexing:
      Keywords: HepTH1-5; ING; In silico analysis; histone modifications; tumour suppressor proteins
    • Accession Number:
      0 (Tumor Suppressor Protein p53)
      0 (Hepcidins)
      0 (Tumor Suppressor Proteins)
    • Publication Date:
      Date Created: 20211222 Date Completed: 20230117 Latest Revision: 20230329
    • Publication Date:
      20230329
    • Accession Number:
      10.1080/07391102.2021.2017349
    • Accession Number:
      34935583