Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain

• Published in: PloS one Vol. 14; no. 5; p. e0216427
• Main Authors: Khan, Md. Imran, Dowarha, Deepu, Katte, Revansiddha, Chou, Ruey-Hwang, Filipek, Anna, Yu, Chin
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 09.05.2019; Public Library of Science (PLoS)
• Subjects: Amino acids; Analysis; Anthranilic acid; Antiproliferatives; Binding; Biochemistry; Biology and Life Sciences; Blocking; Breast cancer; Cancer cells; Cell cycle; Cell Cycle Proteins - chemistry; Cell Cycle Proteins - metabolism; Cell growth; Cell proliferation; Cell Proliferation - drug effects; Chemistry; Complex formation; Enzymes; HCT116 Cells; Humans; Lysozyme; Macrophages; Medicine and Health Sciences; Molecular Docking Simulation; Molecular modelling; Molecular structure; Muramidase - chemistry; Muramidase - metabolism; Neoplasm Proteins - chemistry; Neoplasm Proteins - metabolism; Neoplasms - chemistry; Neoplasms - metabolism; Neoplasms - pathology; NMR; Nuclear magnetic resonance; ortho-Aminobenzoates - pharmacology; Physical Sciences; Physiology; Protein Binding; Protein Domains; Proteins; Receptor for Advanced Glycation End Products; Research and analysis methods; S100 Calcium Binding Protein A6 - chemistry; S100 Calcium Binding Protein A6 - metabolism; Target recognition; China; Taiwan

In this report, using NMR and molecular modeling, we have studied the structure of lysozyme-S100A6 complex and the influence of tranilast [N-(3, 4-dimethoxycinnamoyl) anthranilic acid], an antiallergic drug which binds to lysozyme, on lysozyme-S100A6 and S100A6-RAGE complex formation and, finally, o...