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Spectrum Study on Interactions between Biomolecule and Functionalize Multi-Walled Carbon Nanotubes

Author: XingYueHan
Tutor: SiZhiKun
School: Shandong University
Course: Analytical Chemistry
Keywords: The surface functionalization multi -walled carbon nanotubes Carbon nanotubes - protein interactions Spectroscopy Combinatorial Chemistry Biological Screening
CLC: TB383.1
Type: Master's thesis
Year: 2008
Downloads: 200
Quote: 0
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Abstract


The main subject of application of fluorescence, circular dichroism spectroscopy method to study the surface functionalization of multi-walled carbon nanotubes (f-MWNTs) with a variety of protein interactions, and explore the impact of factors that affect the interaction from protein binding capacity and the the biomolecular level screening of activity inhibition ability of surface functionalization of multi-walled carbon nanotubes library. This research mainly includes the following two aspects: the first part by steady-state fluorescence spectroscopy, time-resolved fluorescence spectroscopy, circular dichroism spectra of the interaction between the f-MWNTs with protein analysis. The surface chemical modification after the f-MWNTs having carboxyl, tyrosine, iso-butylamine and like groups; biomolecule five types of proteins, including BSA, etc.. By various concentrations of f-MWNTs Add the protein solution, and then analyzed the extent of fluorescence quenching of the protein itself, changes in fluorescence lifetime and the protein secondary conformational changes. Binding protein itself, the physical properties of the carbon nanotube surface chemical properties, conducted a comprehensive analysis of the interaction of the protein with f-MWNTs, the following conclusions: 1. Analysis of protein fluorescence quenching, the Stern-Volmer curve joining f-MWNTs after protein fluorescence quenching belongs to static quenching protein with the combination of f-MWNTs is generated stable protein-MWNTs composites; 2. electrostatic adsorption the protein with f-MWNTs interaction plays a vital role. By chemical modification, the surface charge density of the carbon nanotubes has undergone a change, leading to the difference of the different surface-modified carbon nanotubes with the protein interactions; 3. The bulky protein and f-MWNTs binding stronger. The large volume of protein molecules have a larger surface area and more amino acid residues, and provides more space in combination with the f-MWNTs; diameter larger f-MWNTs can be combined with more protein. Larger diameter f-MWNTs having more modifying group, more easily combined with proteins. In addition, the protein in the carbon tube will change their conformation, coordination with the curvature of the carbon tube. The second part of the use of steady-state fluorescence spectra, respectively, from the ability of the protein binding and inhibition of chymotrypsin angle of carbon nanotubes library screening. The screening results showed that the protein binding capacity, most of the ability to bind with various proteins are weak f-MWNTs with a group of chlorobenzene chloride; chymotrypsin inhibition screening results, most of the enzyme The activity inhibiting the larger carbon tube containing N, N-dibutylamine group. To sum up, the papers from the molecular level in vitro study the biological effects of the f-MWNTs found f-MWNTs protein binding has certain selectivity. Protein to determine its physiological function in the life activity (A) is one with its important macromolecules, protein conformation. Therefore, by changing the size of the carbon tubes, the shape, surface charge or the surface chemical groups may be adjusted to its protein binding capacity, thereby reducing the biological toxicity of the carbon nanotubes, to improve their biocompatibility, to ensure that the carbon nanotubes in biomedicine and other fields in application security.

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