Downloads: 13

Files in This Item:
File Description SizeFormat 
d3ra07438b.pdf3.1 MBAdobe PDFView/Open
Title: Chalcone derivatives' interaction with human serum albumin and cyclooxygenase-2
Authors: Karthikeyan, Subramani
Thirunarayanan, Ayyavu
Shano, Leon Bernet
Hemamalini, Arasappan
Sundaramoorthy, Anandh
Mangaiyarkarasi, Rajendiran
Abu, Norhidayah
Ganesan, Singaravelu
Chinnathambi, Shanmugavel  kyouindb  KAKEN_id  orcid (unconfirmed)
Pandian, Ganesh N.
Issue Date: 17-Jan-2024
Publisher: Royal Society of Chemistry (RSC)
Journal title: RSC Advances
Volume: 14
Issue: 4
Start page: 2835
End page: 2849
Abstract: Chalcone derivatives are an extremely valuable class of compounds, primarily due to the keto-ethylenic group, CO–CH[double bond, length as m-dash]CH–, they contain. Moreover, the presence of a reactive α, β-unsaturated carbonyl group confers upon them a broad range of pharmacological properties. Recent developments in heterocyclic chemistry have led to the synthesis of chalcone derivatives, which have been biologically investigated for their activity against certain diseases. In this study, we investigated the binding of new chalcone derivatives with COX-2 (cyclooxygenase-2) and HSA (Human Serum Albumin) using spectroscopic and molecular modeling studies. COX-2 is commonly found in cancer and plays a role in the production of prostaglandin E (2), which can help tumors grow by binding to receptors. HSA is the most abundant protein in blood plasma, and it transports various compounds, including hormones and fatty acids. The conformation of chalcone derivatives in the HSA complex system was established through fluorescence steady and excited state spectroscopy techniques and FTIR analyses. To gain a more comprehensive understanding, molecular docking, and dynamics were conducted on the target protein (COX-2) and transport protein (HSA). In addition, we conducted density-functional theory (DFT) and single-point DFT to understand intermolecular interaction in protein active sites.
Rights: © 2024 The Author(s). Published by the Royal Society of Chemistry
This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
DOI(Published Version): 10.1039/d3ra07438b
PubMed ID: 38234869
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks

Export Format: 

This item is licensed under a Creative Commons License Creative Commons