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Nanoparticle-Protein Interaction Studies Using Spectroscopic and Biophysical Methods

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Title Nanoparticle-Protein Interaction Studies Using Spectroscopic and Biophysical Methods
 
Creator Joshi, Nidhi
Chattopadhyay, Krishnananda
 
Subject Structural Biology & Bioinformatics
 
Description The interaction of nanoparticles with biological interfaces has been studied extensively, where it has been found that proteins form the most abundant class of biomolecules interacting with nanoparticles. Also, nanoparticles due to the huge potential that they offer are being constantly scrutinized for their role in various aspects of biomedical, therapeutic and biotechnological applications. As a matter of fact, the exposure of such particulate matter to living systems is increasing exponentially, raising serious concerns related to their safety. The toxicity due to nanoparticles may arise due to their potential to interact with any biological system, even crossing the most protected blood brain barrier. In addition, they can induce conformational changes in protein, can alter the fluidity of membranes, and may release reactive oxygen species (ROS) and cause severe damage to DNA. Since the potential of nanoparticles are luring, such deleterious manifestations need to be alleviated in order to tap the resource that nanoparticles provide. This is a huge challenge, since nanoparticles are as complex in structure as proteins.
Here, we have developed a novel synthetic approach for the surface modification of one of the most biocompatible magnetite nanoparticles with a more biocompatible surface modifying agent, poly(ethylene) glycol. The stability and the efficiency of the new procedure have been extensively analysed. The interaction of magnetite nanoparticles with different protein systems has been taken in to account. It was observed that bare magnetite nanoparticles affect the proteins differently than that of the surface modified ones. In one of the protein systems, the bare magnetite nanoparticles affect the redox state of the protein; induce intermediate formation and leads to aggregation. The surface modification of nanoparticles maintains the redox state and prevents the aggregation of the protein. In another protein system, the early aggregation kinetics was analysed in the presence of bare and surface modified nanoparticles. Whereas, bare nanoparticles speeds up the aggregation rate, surface modified nanoparticles are found to delay the rate of aggregation.
 
Date 2015
 
Type Thesis
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2326/1/Nidhi_Joshi.pdf
Joshi, Nidhi and Chattopadhyay, Krishnananda (2015) Nanoparticle-Protein Interaction Studies Using Spectroscopic and Biophysical Methods. PhD thesis, Calcutta University.
 
Relation http://www.eprints.iicb.res.in/2326/