ISSN: 1948-5964
+44 1300 500008
Sudha Srivastava
Scientific Tracks Abstracts: JAA
The danger of H5N1 infl uenza virus is not only its high fatality but also its resistance to commercially available drugs. Th e virus contains two surface glycoproteins, haemagglutinin (HA) and neuraminidase (NA). HA is responsible for the binding of the virus to the target cells via the sialic acid residue. NA catalyzes the removal of the terminal sialic acid. NA plays essential role in virus replication. Inhibiting NA can delay the release of progeny virus from infected cells, thereby suppressing the viral population. Th erefore, NA has become the main target for drug design against infl uenza viruses. Most commonly used NA inhibitors currently in the market are oseltamivir and zanamivir. Due to mutations in the active site region NA becomes resistant to oseltamivir. As a part of our ongoing program of developing novel infl uenza virus inhibitors, derivatives of oseltamivir were prepared by modifying the amino group. Th e interactions of these derivatives with neuraminidase have been probed by molecular modeling techniques. Further, the interaction of these derivatives and the eff ect on the thermotropic behaviour and polymorphism of the lipid bilayers has been investigated. Results indicate that the glycyl derivative of oseltamivir has the most profound eff ects on the membrane, compared to the other derivatives and seems to be the most promising derivative for further pharmacological evaluation as a neuraminidase inhibitor.
Dr Sudha Srivastava has done PhD in chemistry from Tata Institute of Fundamental Research, Mumbai and is presently Manager, National Facility for High Field NMR, at TIFR, Mumbai. She is Fellow, National Academy of Sciences. Her major research areas are: NMR studies on intact cells, membrane architecture, drug-design, drug-DNA interactions, conformation and dynamics of bioactive peptides, proteins and hormones. She has more than 130 research publications in refereed journals and is serving as an editorial board member of repute.