Organic solar cells (OSCs) based on bulk-heterojunction have attracted considerable attention because they present some advantages such as low cost, light weight, flexibility and possibility for large area production on plastic substrate. It is believed that, for their commercialization the OSC efficiency should exceed 15% and the charge carrier mobility should exceed 2 cm2/Vs. Therefore, current state of the art in the photovoltaic research activities have been focused on the donor/acceptor bulk heterojunction (BHJ) approach, using a conjugated semi-conducting polymer/oligomer as electron donor (p- type semiconductor) (D) and a fullerene as acceptor (n- type semiconductor) (A) are deposited from a common solvent.

At present most of the acceptor employed in the efficient BHJ organic solar cells are fullerene derivatives (PC61BM or PC71BM) but they are afflicted with a number of significant disadvantages such as electronic tuning via structural modification and weak absorption in the visible spectrum. Moreover, a large electron affinity can result in low open-circuit voltage (VOC). Such disadvantages and problems with fullerenes provide strong incentives to researchers to design and develop new oligomer donor and non-fullerene acceptors that can have crucial photophysical properties such as efficient absorption over the visible spectrum, excellent solubility, high charge carrier mobility and matching energy levels with those of potential donors/acceptors, complementary absorption in the visible region.

The main objective of this proposal is to design and characterization new small molecules both donor (p-type) and acceptors (n-type) organic semiconductors and their potential use in low cost and efficient solution-processed organic bulk-heterojunction solar cells (>10%) with high stability via optimization of morphology of the active layer, interface engineering and using different device architectures.

The nanostructured thermoset block co-polymeric nanocomposite material has been widely investigated in recent years due to their unique properties such as stiffness, strength, rheological properties and barrier action. Polymer matrix must have good process ability so that dispersed particles in the nanometer range can result large improvement in composite properties. Similarly, the incorporation of block co-polymer (nano-filler) in to polymers can render greater reinforcement efficiency than conventional composites. The presence of naofillers can enhance the modulus of rigidity, thermal stability and barrier properties. Generally, the thermoset block co-polymeric nanocomposite materials are two phase systems in which the fillers are dispersed in polymer matrix in nanometer scale. In the nanostructured block co-polymer such as PE-PEO (Polyethylene-polyethylene oxide), PS-PEO (Polystyrene-polyethylene oxide), the polyethylene and polystyrene are hard phase and the polyethylene oxide are soft phase. Thus, the attention will be focused on development of nanostructured thermoset block co-polymeric nanocomposite for various industrial, technological coating applications with respect to curing behaviour.

Despite the growing number of reports linking the toxicity of amyloid proteins with their disruption of membrane integrity, there remains a knowledge gap regarding the molecular determinants by which amyloid-forming proteins aggregate on the membrane or how they act on the membrane to induce membrane permeabilization. Why the permeabilization mechanism varies depending on the protein oligomeric state, or why the nature of the membrane headgroup influences the formation of the protein oligomeric species are yet to be understood. Because of the immense significance of the amyloid formation and the involvement of membranes in the related pathophysiology, it is very important to understand the molecular details of aggregation process, including the role of different lipids whose availability at the cell surface changes with aging and in different pathophysiological conditions (e.g., apoptosis, injury etc). Also, it would be crucial to address show exact sequence requirement for the flibrillation of amyloid-forming proteins.

We will focus on amyloid-forming proteins such as islet amyloid polypeptides (IAPP), ß-amyloid polypeptide, gelsolin and α-synuclein to address the following questions:

(a). Is there any sequence requirement for the aggregation of the amyloid-forming proteins?

(b). What is the role of cholesterol in the aggregation process?

(c). What is the role of lipids which appear at the cell surface during certain pathophysiological condition like apoptosis? We would like to give special attention to understand the role of phosphatidylserine in the aggregation process.

(d). How do these aggregates permeabilize the membrane? In other way, we would like to understand the mechanism of membrane permeabilization induced by amyloids.

This will allow us to decipher the aggregation process of the amyloid-forming proteins at the membrane in a greater detail and we would be able to understand the role of certain lipids in oligomerization event. The proposed project can potentially shed light on the mechanism of membrane permeabilization induced by the aggregates, and therefore pave the way for a better understanding of the event thereby raising the possibility of probing or even checking the process at an early stage of its occurrence.

The majority of viral pathogens that cause emerging and re-emerging infectious diseases are membrane-enveloped viruses, which require the fusion of viral and cell membranes for virus entry. Membrane fusion is the earliest and most important step for any viral fusion. Therefore, antivirals that target the membrane fusion process represent new paradigms for broad-spectrum antiviral discovery. This ‘one bug–one drug’ approach to antiviral drug development can be successful, but it may be inadequate for responding to an increasing diversity of viruses that cause significant diseases in humans. In this project, we would be concentrating on the developing peptide-based broad-spectrum inhibitors of membrane fusion, which will be active for any viral-cell fusion.

An example of successful exploitation of cellular mechanisms to survive in host cell, is provided by the interaction of Mycobacterium species with macrophages. Mycobacteria have evolved ways to avoid the hostile environment of the macrophage. In the case of mycobacteria, observations suggest that phagosomes containing living mycobacterium resist fusion with organelles of the endosomal-lysosomal systems. Analysis of lipid and protein composition of the mycobacterial phagosome show the presence of excess mycolic acids, and coronin 1 that strongly retained on phagosomes harboring viable mycobacteria. The Trp-Asp (WD) repeat-containing coronin 1 is involved in a variety of processes, including signal transduction, motility, cytokinesis, cytoskeletal organization and vesicle fusion. The membrane interaction of the WD proteins will be very important because of the abundance of tryptophan and aspartate in the amino acid sequence.

The major objective of this project is to develop broad spectrum membrane fusion inhibitors utilizing the successful defense mechanism of microbes. This project will particularly focus on coronin 1 that shows a key role in inhibiting the fusion of mycobacterium containing phagosome and lysosome. Coronin 1 contains multiple WD rich conserved sequences, and tryptophan and aspartic acid have unique role in lipid-protein interaction. This encourages us to go for the WD rich conserved peptide sequences and test the fusion inhibitory role of those peptides.