R. Siva Sai Kumar, PhD
Department of Pharmaceutical Chemistry
University of Kansas
Lawrence, KS 66047, USA
Dr. Siva Ratnakaram is a researcher in the field of Biochemistry and Molecular Biology. He received his Ph.D. in Biochemistry from Central Food Technological Research Institute, CSIR, Mysore, India and completed a postdoctoral fellowship at The Pennsylvania State University. He is currently associated with the University of Kansas and working on understanding the structural and functional stability of nanoparticle vaccines via biophysical characterization with an aim to develop protein subunit vaccines for antibiotic resistance pathogenic bacteria.
• (2009) PhD, Biochemistry, University of Mysore
• (2001) MSc, Biochemistry, Sri Venkateswara University
• (1999) BSc, Biology, Sri Venkateswara University
His research interest includes: Protein biochemistry, Biochemical and biophysical characterization of proteins/enzymes, Vaccine development, Upstream and downstream processing of biologics.
Awards and Honors
• (2014), Judge for the 2014 PJAS (Pennsylvania Junior Academy of Science) State Competition at Penn State University’s main campus in University Park, PA
• (2014) Poster session judge for the 17th annual Environmental Chemistry and Microbiology student symposium, 2014 at Penn State University’s campus in University Park, PA.
• Awarded Junior and Senior Research fellowship of Council of Scientific and Industrial Research (CSIR), India, after qualifying a national level competitive examination conducted by CSIR-India.
• (2002), Qualified in GATE (Graduate Aptitude Test in Engineering).
• (2007), American Society for Biochemistry and Molecular Biology (ASBMB), Department of Science and Technology (Central Govt. of India) and Society of Biological Chemists (India) travel fellowship awardee to attend and present research work at the experimental biology 2007 meeting held at Washington DC, USA.
1. Jain A, Hu G, Ratnakaram SSR, Johnson DK, Picking WD, Picking WL, et al. Preformulation characterization and the effect of ionic excipients on the stability of a novel DB fusion protein. Journal of Pharmaceutical Sciences. 2021; 110(1): 108-123. doi: 10.1016/j.xphs.2020.09.008
2. Das S, Howlader DR, Zheng Q, Ratnakaram SSK, Whittier SK, Lu T, et al. Development of a broadly protective, self-adjuvanting subunit vaccine to prevent infections by pseudomonas aeruginosa. Front Immunol. 2020; 11: 583008. doi: 10.3389/fimmu.2020.583008
3. Vullo D, R. Siva Sai Kumar, Scozzafava A, Ferry JG, Supuran CT. Sulphonamide inhibition studies of the β-carbonic anhydrase from the bacterial pathogen Clostridium perfringens. J Enzyme Inhib Med Chem. 2017; 33(1): 31-36. doi: 10.1080/14756366.2017.1388233
4. Yenugudhati D, Prakash D, Kumar AK, Kumar SSR, Yennawar NH, Yennawar HP, et al. Structural and biochemical characterizations of methanoredoxin from methanosarcina acetivorans, a glutaredoxin-like enzyme with coenzyme M-dependent protein disulfide reductase activity. Biochemistry. 2016; 55(2): 313-321. doi: 10.1021/acs.biochem.5b00823
5. Kumar AK, Kumar SSR, Yennawar N, Yennawar H, Ferry JG. Structural and biochemicabl characterization of a ferredoxin: Thioredoxin reductase-like enzyme from methanosarcina acetivorans. Biochemistry. 2015; 54(19): 3122-3128. doi: 10.1021/acs.biochem.5b00137
6. Kumar SSR, Ferry JG. Prokaryotic carbonic anhydrases of earth’s environment. Subcell Biochem. 2014; 75: 77-87. doi: 10.1007/978-94-007-7359-2_5
7. Susan CF, Robert M, eds. Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications. New York, USA: Springer; 2014: doi: 10.1007/978-94-007-7359-2
7. Vullo D, Kumar SSR, Scozzafava A, Capasso C, Ferry JG, Supuran CT. Anion inhibition studies of a β-carbonic anhydrase from Clostridium perfringens. Bioorg Med Chem Lett. 2013; 23(24): 6706-6710. doi: 10.1016/j.bmcl.2013.10.037
8. Kumar SSR, Hendrick W, Corell JB, Patterson AD, Melville SB, Ferry JG. Biochemistry and physiology of the β-Class carbonic anhydrase (Cpb) from clostridium perfringens Strain 13. J Bacteriol. 2013; 195(10): 2262-2269.
9. Kumar SSR, Singh SA, Rao AGA. Conformational stability of α-amylase from malted sorghum (Sorghum bicolor): Reversible unfolding by denaturants. Biochimie. 2009; 91(4): 548-557. doi: 10.1016/j.biochi.2009.01.012
10. Kumar SSR, Vishwanath KS, Singh SA, Rao AGA. Entrapment of α-amylase in alginate beads: Single step protocol for purification and thermal stabilization. Process Biochemistry. 2006; 41: 2282-2288. doi: 10.1016/j.procbio.2006.05.028
11. Kumar SSR, Singh SA, Rao AGA. Thermal stability of alpha amylase from malted jowar (sorghum bicolor). J Agric Food Chem. 2005; 53(17): 6883-6888. doi: 10.1021/jf0501701