Login: Register Home Browse Search My Settings Alerts Help Quick Search Title, abstract, keywords Author e.g. j s smith Journal/book title Volume Issue Page Clear all fields doi:10.1016/j.molstruc.2004.11.076 Copyright © 2004 Elsevier B.V. All rights reserved. Radiation damage of lysozyme in a biomimetic model: some insights by Raman spectroscopy Armida Torreggiani a, , , Maurizio Tamba a, , Immacolata Manco b, , Maria Rosaria Faraone-Mennella b, , Carla Ferreri a, and Chryssostomos Chatgilialoglu a, a Istituto ISOF, Consiglio Nazionale delle Ricerche, Via P. Gobetti 101, Bologna 40129, Italy b Dip. Chimica Biologica, Università di Napoli, via Mezzocannone 16, Napoli 80134, Italy Received 7 September 2004; revised 18 November 2004; accepted 18 November 2004. Available online 11 January 2005. Journal of Molecular Structure Volumes 744-747, 3 June 2005, Pages 767-773 MOLECULAR SPECTROSCOPY AND MOLECULAR STRUCTURE 2004 SummaryPlus Full Text + Links PDF (150 K) View thumbnail images | View full size images Related Articles in ScienceDirect View More Related Articles View Record in Scopus Cited By in Scopus (3) Abstract A biomimetic model for protein/lipid radical damage is described. The model shows that the protein degradation is accompanied by trans lipid isomerization due to thiyl radicals, derived from sulfur- containing residues and diffused through the lipid bilayer. γ-Irradiation was used to obtain free radical generation and lysozyme was chosen as enzyme example. A detailed study of the Raman spectra of lysozyme irradiated at different doses coupled to vesicle experiments, as well as enzymatic assays, is reported to gather a comprehensive view of the irradiation effect. The lysozyme resistance to degradation by γ-irradiation is remarkable and the protein structure play a significant role in blocking the ready access of free radicals both to the sulfur-containing residues and the active site. The degradation of sulfur moieties does not occur immediately, but as irradiation progressed, the involvement of these residues takes place. In fact, structural changes induced on the protein render these residues more exposed and susceptible of radical attack. Tyr are confirmed to be among the most sensitive residues towards oxidation. These results can be relevant for a better understanding of mechanisms of tandem radical damages occurring in a biological environment. Keywords: Lysozyme; γ-Irradiation; Raman spectroscopy; Radical damage; Trans lipid Article Outline 1. Introduction 2. Experimental 2.1. Materials and methods 2.2. γ-Irradiation of DOPC-Lyso vesicles 2.3. γ-Irradiation of Lyso in aqueous solution 2.4. Activity assays 3. Results and discussion Spectrophotometric studies on the binding of Vitamin C ... Journal of Luminescence Conformational effects in the high- performance liquid c... Journal of Chromatography A Thermal behavior of proteins in high-performance hydrop... Journal of Chromatography A Ce3+-doped lutetium yttrium orthosilicate crystals: Str... Materials Science and Engineering: B Binding analysis of farrerol to lysozyme by spectroscop... Spectrochimica Acta Part A: Molecular and Biomolecular ... Page 1 of 10 ScienceDirect - Journal of Molecular Structure : Radiation damage of lysozyme in a biom... 27/10/2012 mhtml:file://C:\Documents and Settings\UserXP\Desktop\abilitazione 2012\abilitaz files ...