Dr. Ashis Biswas

Dr. Ashis Biswas |Clyto Access

School of Basic Sciences, IIT Bhubaneswar, India


Expertise: Biophysical Chemistry, Biochemistry and Molecular biology of small heat shock proteins.


Dr. Ashis Biswas graduated with Chemistry (Honours) from Jadavpur University, Kolkata in 1996. He did his post graduation in Physical Chemistry from the same university in 1998. Then, he worked as a project scholar in Department of Chemistry, IIT Kharagpur till 2000. In 2001, he joined the group of Prof. Kalipada Das in Bose Institute, Kolkata to pursue Ph.D and obtained the degree in 2006. He also did postdoctoral research at Case Western University, USA and Cleveland Clinic, USA. In 2009, he joined as Assistant Professor at Department of Chemistry, NIT Rourkela. In 2010, he moved to IIT Bhubaneswar and presently working as Assistant Professor at School of Basic Sciences. He has 38 research publications to his credit which has been published in international and national journals of repute.



Title: Mycobacterium leprae HSP18: An alternative drug targeting strategy for the treatment of leprosy


Leprosy is caused by Mycobacterium leprae (M. leprae), an obligate intracellular pathogen that is unique in its ability to invade the peripheral nervous system. For the treatment of leprosy, different drugs are available which are used in multidrug therapies (MDT). But MDT possesses numerous side effects like abdominal severe pain, skin decolourization, liver problems, blood in urine , stools etc. Therefore, new avenues are being explored by the scientists for the treatment of leprosy with minimal side effects. In order to find out an effective cure for leprosy, various antigens/mycobacterial proteins are constantly studied as drug targets. Among these antigenic proteins highly expressed in M. leprae, the 18 kDa antigen (later known as HSP18) has deserved special attention as this protein is found to stimulate both human and murine T-cells as well as B-cells. HSP18 has been initially identified as a membrane protein and it is specifically activated during the intracellular growth of M. leprae. HSP18 belongs to the class of small heat shock proteins (sHSPs) and exhibits chaperone activity. It is believed that the chaperone function of M. leprae HSP18 plays a crucial role in the survival and virulence of M. leprae pathogen in different phases of leprosy. Recently, our group has shown that ATP binds reversibly to the ß4-ß8 groove/strands of HSP18 with a binding affinity in sub-micromolar range. Such moderate reversible interaction perturbs its conformations as well as enhances its chaperone function. This study provides a new basis for the development of new drug targeting strategy such as ATP competitive antibiotics/inhibitors in context of effective treatment of leprosy. An alternative treatment of leprosy using nanoparticles is of special importance as nanoparticles can invade the thick cell wall of mycobacterial species consisting of mycolic acids which is impermeable to many drugs as well as small molecules. Lowering of chaperone activity of HSP18 upon the interaction with silver nanoparticle provides a clue for using silver nanoparticle for effective treatment of leprosy. Structure-function studies of this sHSP in presence of various small molecules (AMP, ADP, ATP, silver nanoparticle etc.) and their consequences in influencing this particular disease will be discussed extensively during the presentation.


Related Conferences :

International Biotechnology and Pharmaceutical Industry Forum