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Assay of protein and peptide adducts of cholesterol ozonolysis products by hydrophobic and click enrichment methods |pdf=|usr=}}{{25185119 }} gab.com Text Assay of protein and peptide adducts of cholesterol ozonolysis products by hydrophobic and click enrichment methods JO: Chem Res Toxicol http://www.kidney.de/pget.php?&tw=1&pmid=25185119 #FOAvip Cholesterol undergoes ozonolysis to afford a variety of oxysterol products, including cholesterol-5,6-epoxide (CholEp) and the isomeric aldehydes secosterol A (seco A) and secosterol B (seco B). These oxysterols display numerous important biological activities, including protein adduction; however, much remains to be learned about the identity of the reactive species and the range of proteins modified by these oxysterols. Here, we synthesized alkynyl derivatives of cholesterol-derived oxysterols and employed a straightforward detection method to establish secosterols A and B as the most protein-reactive of the oxysterols tested. Model adduction studies with an amino acid, peptides, and proteins provide evidence for the potential role of secosterol dehydration products in protein adduction. Hydrophobic separation methods-Folch extraction and solid phase extraction (SPE)-were successfully applied to enrich oxysterol-adducted peptide species, and LC-MS/MS analysis of a model peptide-seco adduct revealed a unique fragmentation pattern (neutral loss of 390 Da) for that species. Coupling a hydrophobic enrichment method with proteomic analysis utilizing characteristic fragmentation patterns facilitates the identification of secosterol-modified peptides and proteins in an adducted protein. More broadly, these improved enrichment methods may give insight into the role of oxysterols and ozone exposure in the pathogenesis of a variety of diseases, including atherosclerosis, Alzheimer's disease, Parkinson's disease, and asthma. Twit Text FOAVip Assay of protein and peptide adducts of cholesterol ozonolysis products by hydrophobic and click enrichment methods ????Chem Res Toxicol http://www.kidney.de/pget.php?&tw=1&pmid=25185119 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25185119 #FOAvip English Wikipedia <ref>{{Cite pmid|25185119 }}</ref> Assay of protein and peptide adducts of cholesterol ozonolysis products by hydrophobic and click enrichment methods #MMPMID25185119 Windsor K ; Genaro-Mattos TC ; Miyamoto S ; Stec DF ; Kim HY ; Tallman KA ; Porter NA Chem Res Toxicol 2014[Oct]; 27 (10 ): 1757-68 PMID25185119 show ga Cholesterol undergoes ozonolysis to afford a variety of oxysterol products, including cholesterol-5,6-epoxide (CholEp) and the isomeric aldehydes secosterol A (seco A) and secosterol B (seco B). These oxysterols display numerous important biological activities, including protein adduction; however, much remains to be learned about the identity of the reactive species and the range of proteins modified by these oxysterols. Here, we synthesized alkynyl derivatives of cholesterol-derived oxysterols and employed a straightforward detection method to establish secosterols A and B as the most protein-reactive of the oxysterols tested. Model adduction studies with an amino acid, peptides, and proteins provide evidence for the potential role of secosterol dehydration products in protein adduction. Hydrophobic separation methods-Folch extraction and solid phase extraction (SPE)-were successfully applied to enrich oxysterol-adducted peptide species, and LC-MS/MS analysis of a model peptide-seco adduct revealed a unique fragmentation pattern (neutral loss of 390 Da) for that species. Coupling a hydrophobic enrichment method with proteomic analysis utilizing characteristic fragmentation patterns facilitates the identification of secosterol-modified peptides and proteins in an adducted protein. More broadly, these improved enrichment methods may give insight into the role of oxysterols and ozone exposure in the pathogenesis of a variety of diseases, including atherosclerosis, Alzheimer's disease, Parkinson's disease, and asthma. |Aldehydes/chemistry [MESH] |Amino Acid Sequence [MESH] |Biotin/chemistry [MESH] |Cholesterol/analogs & derivatives/*chemistry [MESH] |Chromatography, High Pressure Liquid [MESH] |Click Chemistry [MESH] |Cytochromes c/chemistry [MESH] |Humans [MESH] |Hydrophobic and Hydrophilic Interactions [MESH] |Isomerism [MESH] |Molecular Sequence Data [MESH] |Ozone/*chemistry [MESH] |Peptides/analysis/*chemistry [MESH] |Proteins/*chemistry [MESH] |Serum Albumin/chemistry [MESH] |Solid Phase Extraction [MESH] |Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization [MESH]Assay of protein and peptide adducts of cholesterol ozonolysis product(epmc).pdf DeepDyve Pubget Overpricing