Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain.
Cell Cycle Proteins
/ chemistry
Cell Proliferation
/ drug effects
HCT116 Cells
Humans
Molecular Docking Simulation
Muramidase
/ chemistry
Neoplasm Proteins
/ chemistry
Neoplasms
/ chemistry
Protein Binding
Protein Domains
Receptor for Advanced Glycation End Products
S100 Calcium Binding Protein A6
/ chemistry
ortho-Aminobenzoates
/ pharmacology
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
16
01
2019
accepted:
20
04
2019
entrez:
10
5
2019
pubmed:
10
5
2019
medline:
15
1
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31071146
doi: 10.1371/journal.pone.0216427
pii: PONE-D-19-01542
pmc: PMC6508705
doi:
Substances chimiques
AGER protein, human
0
Cell Cycle Proteins
0
Neoplasm Proteins
0
Receptor for Advanced Glycation End Products
0
S100 Calcium Binding Protein A6
0
ortho-Aminobenzoates
0
S100A6 protein, human
105504-00-5
Muramidase
EC 3.2.1.17
tranilast
HVF50SMY6E
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0216427Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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