Ramteke , S.N. and Ginotra , Y.P. and Walke, G.R. and Joshi , B.N. and Kumbhar , A.S. and Rapole , S. and Kulkarni , P.P. (2013) Eff ects of oxidation on copper-binding properties of A b 1-16 peptide: A pulse radiolysis study. Free Radical Research, 47 (12). pp. 1046-1053.

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Abstract

The reaction of hydroxyl radicals ( • OH) with A β 1-16 peptide was carried out using pulse radiolysis to understand the eff ect of oxidation of peptide on its copper-binding properties. This reaction produced oxidized, dimeric and trimeric A β 1-16 peptide species. The formation of these products was established with the help of fl uorescence spectroscopy and mass spectrometry. The mass spectral data indicate that the major site of oxidation is at His6, while the site for dimerization is at Tyr10. Diethyl pyrocarbonate-treated A β 1-16 peptide did not produce any trimeric species upon oxidation with • OH. The quantitative chemical modifi cation studies indicated that one of the three histidine residues is covalently modifi ed during pulse radiolysis. The copper-binding studies of the oxidized peptide revealed that it has similar copperbinding properties as the unoxidized peptide. Further, the cytotoxicity studies point out that both oxidized and unoxidized A β 1-16 peptide are equally effi cient in producing free radicals in presence of copper and ascorbate that resulted in comparable cell death.

Item Type:	Article
Additional Information:	This is Online Free Journal (for full text click above website)
Subjects:	Bioinformatics and Proteomics
Depositing User:	Mr. Rameshwar Nema
Date Deposited:	24 Apr 2015 07:19
Last Modified:	06 Jul 2015 06:05
URI:	http://nccs.sciencecentral.in/id/eprint/121

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