ABSTRACT
Lipid peroxidation is responsible for the generation of chemically reactive, diffusible lipid-derived electrophiles (LDEs) that covalently modify cellular protein targets. These protein modifications modulate protein activity and macromolecular interactions and induce adaptive and toxic cell signaling. Protein modifications induced by LDEs can be identified and quantified by affinity enrichment and liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based techniques. Tagged LDE analog probes with different electrophilic groups can be covalently captured by click chemistry for LC-MS/MS analyses, thereby enabling in-depth studies of proteome damage at the protein and peptide sequence levels. Conversely, click-reactive, thiol-directed probes can be used to evaluate thiol damage caused by LDE by difference. These analytical approaches permit systematic study of the dynamics of protein damage caused by LDE and mechanisms by which oxidative stress contribute to toxicity and diseases.
Subject(s)
Lipid Peroxidation , Proteome/metabolism , Proteomics/methods , Chromatography, Liquid , Humans , Protein Processing, Post-Translational , Proteome/analysis , Tandem Mass SpectrometryABSTRACT
The suppression of chaos in an one-dimensional model of malignant tumor growth is presented. As a result, a steady-state and differentperiodic motions, embedded in the chaotic attractor, arestabilized.
ABSTRACT
A model of competition between populations of two species, describedby a two dimensional map, is analytically and numerically studied. A rich dynamics is observed.
