International Journal of
Physical Sciences

  • Abbreviation: Int. J. Phys. Sci.
  • Language: English
  • ISSN: 1992-1950
  • DOI: 10.5897/IJPS
  • Start Year: 2006
  • Published Articles: 2572

Full Length Research Paper

A study on the electronic and structural properties of fullerene C36 and it’s interaction with amino acid

Fereshteh Naderi1*, Somayyeh Rostamian2 and Behjat Naderi2
  1Department of Chemistry, Shahr_e Qods Branch, Islamic Azad University, Tehran, Iran. 2Shahr_e Qods Branch, Islamic Azad University, Tehran, Iran.
Email: [email protected]

  •  Accepted: 29 February 2012
  •  Published: 23 March 2012

Abstract

 

C36 is the most important fullerene cage. In this paper, the structural properties of C36fullerene interacting with glycine radicals are analyzed through the density functional theory. The radical adsorptions result in modifications on the structural properties of the original fullerene. It was found out that the binding of glycine to C36 generated a slightly unstable complex. This indicates that fullerene cages might be unable to form stable bindings to glycine radicals. These results are extremely relevant in order to identify the potential applications of functionalized C36 as drug delivery systems.

 

Key words: C36, glycine, density functional theory, formation energy, highest occupied molecular orbital-lowest unoccupied molecular orbital (HOMO-LUMO) gap.

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This article is published under the terms of the Creative Commons Attribution License 4.0

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