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National Symposium on Biophysics &
Golden Jubilee Meeting of Indian Biophysical Society
 JPP40
tendency to acquire helical conformation in helix inducing
solvent 2,2,2- trifluoroethanol. Overall the increase in
cationic charge of o.-MSH improved Staphylocidal
activity and membrane damaging efficacy of the pep tides
without compromising their cell selectivity. It also
indicated that electrostatic interactions and ability to
acquire ordered conformation may be crucial for o.-MSH
and its analogues to selectively disrupt microbial
membrane leading to bacterial cell death without
harming host cell membrane.
Structure based Function Prediction of
Hypothetical Proteins from Neisseria gonorrhoeae
OP 21
Kundan Kumar, Amresh Prakash, Asimul Islam, Faizan
Ahmad, and Md. Imtaiyaz Hassan'
Centre for Interdisciplinary Research in Basic Sciences, lamia Millia
Islamia, New Delhi-ll 0025, India
Neisseria gonorrhoeae is a Gram-negative bacteria
predominantly causes a sexually transmitted infection
known as gonorrhoea. The frequent emergence of new
multiple drug resistant strain need the extensive study
of its genome and development of new drug/vaccine
against these pathogen. After analysis of the proteome
data of N. gonorrhoeae we found that a large fraction
proteome are listed as conserved hypothetical protein
(HP) for which function are still not known. Study of these
HPs offers presentation of new structures and novel
functions of HPs and also new cascade of biochemical
pathways. Furthermore, new HPs may be serving as
markers and pharmacological targets. We have identiued
10 HPs showing lyases activity from N. gonorrhoeae from
sequence analysis and performed homology modeling to
reveal the structural basis of the function, structural
motifs and amino acids involved in catalytic sites. Along
with this, function may be inferred on the basis of
properties that are associated with a speciuc functional
class and family of the proteins. We also studied the sub-
cellular localization and presence of signal peptide in the
HPs. Moreover, sequence analysis was also performed
to find out the physicochemical properties including
amino acid composition, aliphatic index and instability
index of HPs. Finally, function annotation and
identiucation of functionally important regions in HPs
from N. gonorrhoeae may leads to better understanding
of its virulence mechanism, adaptability in host system,
tolerance for host immune system and emergence of
drugs resistance strain and finally drug/ vaccine
discovery.
E-mail: mihassan@jmi.ac.in
Study of dynamics of Protein Nanoparticle
complex in aqueous medium using Impedance
spectroscopy OP 22
Mahesh Samant, Bipin Khade, H Muthurajan* P M
Dongre
Department of Biophysics, University of Mumbai, Santacruz (E),
Mumbai 400098
*Natiollal Centre for Nanosciences and Nanotechnology, University
of Mumbai, Mumbai 400098
A rapid development of nanosciences and
nanotechnology offers nanoparticles great applications in
various fields, like drug development, materials for drug
delivery and biosensors etc. Nanoparticles possesses a
unique physicho-chemical properties such as optical,
magnetic, large surface to volume ratio etc. Nanoparticles
also confer properties of enhanced bioavailability and
improved solubility. When nanoaprticles enters in
biological fluids, it leads undesired effects. The effects
mayor may not favour to the systems. Hence it is prime
important to understand interaction between
nanoaprticles and biological materials like proteins,
enzymes and nucleic acids etc.
In the present investigation we studied the nanoparticle-
protein complex using dielectric spectroscopy. Dielectric
spectroscopy reveals typical signature of relaxation
process of aqueous media namely dielectric constant,
dielectric loss which commonly known as a., p, y and 8
relaxation.
The Chemical route synthesized Silver Nanoparticles
were characterized using Dynamic Light Scattering (DIS),
Transmission Electron Microscope (TEM) and UV visible
spectroscopy. The protein nanoparticles complex was
confirmed by fluorescence and UV visible spectroscopy.
The Frequency dependent Dielectric dispersion of Silver
NP's and Silver NP-protein complex was investigated in
the temperature range of 263K - 373K and in a frequency
range of 20Hz - 2MHz by impedance spectroscopy
(Agilent LCR component analyzer). Variation in dielectric
constant (s') and dielectric loss (s") was observed
nanopartilce and protein and Protein-nanoaparticle
complex. Bode plot (impedance vs frequency) showed
increased in impedance (Z) of protein-npts complex.
Average relaxation time ('r) for a-region (20HZ-100KHZ)
and p-region ( > 200 KHZ) was tabulate in control and
test condition as a function of reciprocal temperature. In
addition, the electrical conductivity was monitored. The
several relaxation processes were attributed to motions
that range from side groups of the proteins in the aqueous
medium.
E-mail: samant.mahesh77@gmail.com