TY - JOUR
T1 - Lysozyme as the anti-proliferative agent to block the interaction between S100A6 and the RAGE V domain
AU - Imran Khan, Md
AU - Dowarha, Deepu
AU - Katte, Revansiddha
AU - Chou, Ruey Hwang
AU - Filipek, Anna
AU - Yu, Chin
N1 - Funding Information:
This work was supported by the Ministry of Science and Technology (MOST) of Taiwan (grant number MOST 104–2113-M-007-019-MY3, MOST 107–2113-M-007-008), MOST 105-2320-B-039-059-MY3 and MOHW107-TDU-B-212-114025 from Ministry of Health and Welfare (MOHW), and the Drug Development Center, China Medical University from The Featured Areas Research Center Program within the framework of the Higher Education Sprout Project by the Ministry of Education (MOE) in Taiwan. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. We acknowledge the Department of Chemistry, National Tsing Hua University, for providing the Facility of Nuclear Magnetic Resonance, 700MHz, and humbly thank all the members who contributed to this research work.
Publisher Copyright:
© 2019 Khan et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
PY - 2019/5
Y1 - 2019/5
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/85065671146
UR - https://www.scopus.com/pages/publications/85065671146#tab=citedBy
U2 - 10.1371/journal.pone.0216427
DO - 10.1371/journal.pone.0216427
M3 - Article
C2 - 31071146
AN - SCOPUS:85065671146
SN - 1932-6203
VL - 14
JO - PloS one
JF - PloS one
IS - 5
M1 - e0216427
ER -
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