Chaiyos Sirithanakorn, Ph.D.
Instructor, Faculty of Medicine
King Mongkut’s Institute of Technology Ladkrabang
B.Sc. (Biotechnology), 2010
Department of Applied Biology, Faculty of Science, King Mongkut’s Institute of Technology Ladkrabang
Ph.D. (Biochemistry), 2016
Department of Biochemistry, Faculty of Science, Mahidol University
Faculty of Pharmaceutical Science, Chulalongkorn University
Visiting Research Scholar
Molecular Enzymology Laboratory, University of Western Australia
Postdoctoral Research Associate, (Feb 2020 – present)
Department of Microbiology, School of Molecular & Cellular Biology
University of Illinois at Urbana Champaign, USA
My laboratory is interested in two main research topics:
The molecular metabolism of sulfur containing vitamins including biotin & lipoic acid and their related enzyme cofactors. We use mainly in Escherichia coli as a model for study but not limited to other biosynthetic microorganisms. We found that both vitamins are essential for bacterial growth and virulence. Understanding the metabolism of them (in both pathogenic bacteria and human) would be shed light on the development of alternative antibiotic drug targeting enzymes in their synthesis and/or attachment.
Identification and analysis of bioactive peptides from natural source or obtained from synthetic biology. Bioactive peptides are small peptides composed of between 3 to 20 amino acid residues. They have various biological properties such as antimicrobial, antioxidant, immunomodulatory, anti-inflammatory, and etc. This information may provide fundamental insights and also lead to opportunity for therapeutic development.
1. Chaiyos Sirithanakorn, Sarawut Jitrapakdee, and Paul V. Attwood (2016) Investigation of the Roles of Allosteric Domain Arginine, Aspartate, and Glutamate Residues of Rhizobium etli Pyruvate Carboxylase in Relation to Its Activation by Acetyl CoA. Biochemistry 55, 4220-4228.
2. Choosangtong K., Sirithanakorn C., Adina-Zada A., Wallace J.C., Jitrapakdee S. and Attwood P.V. (2015) Residues in the acetyl-CoA binding site of pyruvate carboxylase involved in allosteric regulation. FEBS Lett. 589, 2073-2079.
3. Sirithanakorn C., Adina-Zada A., Wallace J.C., Jitrapakdee S., and Attwood P.V. (2014) Mechanisms of Inhibition of Rhizobium etli Pyruvate Carboxylase by L-Aspartate, Biochemistry 53, 7100-7106.