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Volume 5, Issue 5 Res. Rev. J Mat. Sci. 2017
ISSN: 2321-6212 Advanced Materials 2017
September 07-08, 2017
September 07-08, 2017 | Edinburgh, Scotland
Advanced materials & Processing
11th International Conference on
Structures, interactions and optical responses from polymer and polymer nanocomposites
Sarathi Kundu
Institute of Advanced Study in Science and Technology, India
Biological functions of biopolymers like proteins strongly depend upon their structures which can be modified by the interactions
with surrounding environments. Understandingprotein-protein interactions in solutions are very important as it helps inobtaining
protein crystals, biochemical roles of proteins, ideas about some diseases like Alzheimer, Parkinson, etc. Biochemical functions of
proteins are regulated in the presence of ions around them and hence the effect of ionic strength, nature of ions, temperature, pH,
concentration, nanoparticles, etc. strongly affect the protein-protein interactions. Among different proteins, globular proteins like
BSA, HSA, lysozyme can be considered as charged, colloidal particles and both short-range attraction and long-range electrostatic
repulsion exists among the protein molecules in solution and hence Derjaguin-Landau-Verway-Overbeek (DLVO) potential can
be applied to obtain the interaction nature and to explain the phase behaviors. However, DLVO model cannot fully explain the
rich behavior of proteins due to the presence of inhomogeneous surface charges and irregular shape of proteins. One, two or three
attractive or repulsive Yukawa form potentials were also used to explain the nature of interactions. Small angle neutron scattering
(SANS) study shows that in combination with the short-range attraction and intermediate-range electrostatic repulsion, a possible
weak long-range attractive interaction between protein molecules may exist. SANS study also shows that for different counterions and
for the equal ionic strength, the interactions are largely modified by the tri-valent (Fe3+) and di-valent (Ni2+ ) ions and comparatively
less by the mono-valent (Na+) ions. Below the isoelectric point, protein has a net positive surface charge although local charge
inhomogeneity presents and as a result interaction nature modifies. In presence of different ions, cold gelation behaviors of proteins
have also been studied which indicates the fractal structure formation after gelation. In presence of charged polymers, conformational
changes of globular proteins may occur depending upon the charge states of the polyelectrolytes. Protein-polyelectrolyte complexes
(PPC) show modified behaviors than that of pure protein/polymer. It has been observed that the thin films of PPC show a larger red-
shift in the fluorescence emissions in comparison with that of pure protein. Protein and protein films are also used as templates to
form metallic nanostructures of different shapes and sizes which are also used for modifying both optical and electrical properties.
Biography
Dr. Sarathi Kundu did his . from Visva-Bharati University, West Bengal. He completed his Ph.D. work from Saha Institute of Nuclear Physics, Kolkata in 2006
and the degree is conferred by Jadavpur University. He did is Post-Doctoral research work from University of Paris Sud, France. He was Visiting Faculty Fellow in
S.N. Bose National Centre for Basic Sciences, Kolkata and Visiting Scientist in KEK, Japan. At present he is Associate Professor in IASST, Guwahati. Dr. Kundu has
been working on soft matter physics with emphasis on organic thin films and nanomaterials. He is interested to explore structures and properties using scattering,
spectroscopic and microscopic methods. Dr. Kundu has published nearly 50 journal papers so far.
Sarathi Kundu, Res. Rev. J Mat. Sci. 2017, 5:5
DOI: 10.4172/2321-6212-C1-005