Conformational study of bovine a-lactalbumin and glucosidase mediated by metal and metal oxide nanoparticles.

Dr. Subhankar Paul Information Under Updation*

  • Project code : BT/PR13853/NNT/28/481/2010
  • Designation : Professor
  • Department :Biotechnology and Medical Engineering
  • Affiliation : National Institute of Technology, Rourkela
  • Email Id :spaul@nitrkl.ac.in
  • Sanctioned Amt :Rs. 24,86,528/-
  • Sanctioned Date :2012-03-13
  • Completion Date :2015-03-13
  • Web Url : https://www.researchgate.net/profile/Subhankar_Paul2
  • Project Status :Completed

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Objectives of the Study

1. Study the in vitro urea and GdnHCl-mediated unfolding. 

2. Preparation of ZnO, Ag and Au NPs with various size and shapes. 
3. Observe the in vivo expression and extent of folding of a-LA and BGL in presence of NPs. 
4. Refolding of a-LA nad BGL in presence of NPs under various conditions.

Proposed outcomes of the study

Although NP and protein interaction study was carried out with proteins like lysozyme, -lactalbumin, BSA, no such study has yet been carried out on a-LA or BGL. The number of proteins so far has been studied in this regard is less and more such related investigations should be carried out to understand the common strategy if any that how metal NPs with various sizes and shapes interact with proteins and what is the possible consequence of the structural perturbation of the proteins. While unfolding study of the above-mentioned proteins in the presence of NPs has been reported, no refolding study of these proteins has yet been carried out under the similar condition. Therefore, unfolding and refolding study of bovine a-LA and BGL may be hugely helpful to find informations for understanding the future applications of NP-protein conjugate based use as drug. Based on the relevant informations and requirement the investigators have expected to get the following outcome from the proposed project: 

1. The successful completion of the project may provide informations that will help in clear understanding the metal/metal oxide nanoparticles and protein interaction in vitro. 
2. The study will help in understanding the metal/metal oxide nanoparticles and protein interaction in vivo (E.coli) and developing the idea how in vivo folding of recombinant protein can be influenced by metal NPs. 
3. Open up the possibility of manufacturing new drugs based on the understanding how they interact with various proteins in the body and the subsequent consequence. 
4. The probable structural changes of proteins mediated by metal NPs both in vivo and in vitro may enrich the protein folding research activities in the country and internationally. 
5. May open up the future of using NP- protein conjugate in place of a-LA-oleic acid complex acts as antitumor agents.

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