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Aims: c-Myc, along with its partner MAX, regulates the expression of several genes, leading to an oncogenic phenotype. The MAX interacting interface of c-Myc is disordered and uncharacterized for small molecule binding. Salvianolic acid B possesses numerous therapeutic properties, including anticancer activity. The current study was designed to elucidate the interaction of the Sal_Ac_B with the disordered bHLH domain of c-Myc using computational and biophysical techniques. Materials & methods: The binding of Sal_Ac_B with Myc was studied using computational and biophysical techniques, including molecular docking and simulation, fluorescence lifetime, circular dichroism and anisotropy. Results & conclusions: The study demonstrated a high binding potential of Sal_Ac_B against the disordered Myc peptide. The binding of the compounds leads to an overall conformational change in Myc. Moreover, an extensive simulation study showed a stable Sal_Ac_B/Myc binding.

Original publication




Journal article


Future Med Chem

Publication Date





1341 - 1352


MD simulations, c-Myc/MAX heterodimer, fluorescence lifetime, salvianolic Acid B, time-resolved anisotropy, Anisotropy, Antineoplastic Agents, Benzofurans, Binding Sites, Circular Dichroism, Humans, Models, Molecular, Molecular Conformation, Proto-Oncogene Proteins c-myc, Spectrometry, Fluorescence