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

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...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2019-05, Vol.14 (5), p.e0216427
Main Authors: Khan, Md Imran, Dowarha, Deepu, Katte, Revansiddha, Chou, Ruey-Hwang, Filipek, Anna, Yu, Chin
Format: Article
Language:English
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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, on cell proliferation. We have found that tranilast may block the S100A6-lysozyme interaction and enhance binding of S100A6 to RAGE. Using WST1 assay, we have found that lysozyme, most probably by blocking the interaction between S100A6 and RAGE, inhibits cell proliferation while tranilast may reverse this effect by binding to lysozyme. In conclusion, studies presented in this work, describing the protein-protein/-drug interactions, are of great importance for designing new therapies to treat diseases associated with cell proliferation such as cancers.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0216427