Panida Boontawee
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Panida Boontawee has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Kritsada Pruksaphon
Walailak University
1 shared publication - Nopawit Khamto
Department of Biochemistry, Faculty of Medical Science, Naresuan University, Phitsanulok 65000, Thailand
1 shared publication - Nuttee Suree
Division of Biochemistry and Biochemical Innovation, Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand
1 shared publication - Panchika Prangkio
Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand
1 shared publication - Puttinan Meepowpan
Department of Chemistry, Faculty of Science, Chiang Mai University, 239 Huay Kaew Road, Chiang Mai 50200, Thailand
1 shared publication - Suwicha Patnin
Laboratory of Organic Synthesis, Chulabhorn Research Institute, Bangkok 10210, Thailand
1 shared publication
Latest Publications
- Open Access
- 7 October 2025
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 26 (19) , 9742
Discovery of Galloyl–Flavonoid Conjugates as SARS-CoV-2 3CLpro Inhibitors: Understanding Binding Interactions Through Computational Approaches
The emergence of SARS-CoV-2 in 2019 posed significant global public health challenges. One of the most promising targets for novel antiviral drug development is the SARS-CoV-2 main protease (3CLpro). In this study, fragment molecular orbital (FMO) calculations were conducted to provide guidance for the structural modification of natural flavonoids, identifying the pyrogallol moiety as a key candidate. Natural flavonoids were chemically modified to generate 33 semi-synthetic derivatives through the introduction of various functional groups. Our findings revealed that the incorporation of a galloyl moiety significantly enhances anti-proteolytic activity against SARS-CoV-2 3CLpro, achieving up to a 23-fold increase compared to the activity of the parent compounds. Notably, 7-O-galloyl-DMC (40) exhibited the highest anti-proteolytic activity in an enzymatic assay. Additionally, molecular dynamics simulations provided atomic-level insights into the interactions between the galloyl moiety and 3CLpro. All galloylated flavonoid derivatives positioned their galloyl groups within the S1′ sub-pocket, facilitating hydrogen bonding and π-interactions, particularly with Thr26 and Leu27. These findings underscore the potential of the galloyl moiety as a crucial structural element for enhancing the binding affinity of flavonoids with inhibitory activity against SARS-CoV-2 3CLpro.
- 7 October 2025
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 26 (19) , 9742
Open AccessDiscovery of Galloyl–Flavonoid Conjugates as SARS-CoV-2 3CLpro Inhibitors: Understanding Binding Interactions Through Computational Approaches
The emergence of SARS-CoV-2 in 2019 posed significant global public health challenges. One of the most promising targets for novel antiviral drug development is the SARS-CoV-2 main protease (3CLpro). In this study, fragment molecular orbital (FMO) calculations were conducted to provide guidance for the structural modification of natural flavonoids, identifying the pyrogallol moiety as a key candidate. Natural flavonoids were chemically modified to generate 33 semi-synthetic derivatives through the introduction of various functional groups. Our findings revealed that the incorporation of a galloyl moiety significantly enhances anti-proteolytic activity against SARS-CoV-2 3CLpro, achieving up to a 23-fold increase compared to the activity of the parent compounds. Notably, 7-O-galloyl-DMC (40) exhibited the highest anti-proteolytic activity in an enzymatic assay. Additionally, molecular dynamics simulations provided atomic-level insights into the interactions between the galloyl moiety and 3CLpro. All galloylated flavonoid derivatives positioned their galloyl groups within the S1′ sub-pocket, facilitating hydrogen bonding and π-interactions, particularly with Thr26 and Leu27. These findings underscore the potential of the galloyl moiety as a crucial structural element for enhancing the binding affinity of flavonoids with inhibitory activity against SARS-CoV-2 3CLpro.