Determination of Potential 4-hydroxy-2-nonenal Covalent Binding Sites on Electron Transfer Flavoprotein using Liquid Chromatography-Mass Spectrometry by Margaret Breen-Lyles

Determination of Potential 4-hydroxy-2-nonenal Covalent Binding Sites on Electron Transfer Flavoprotein using Liquid Chromatography-Mass Spectrometry by Margaret Breen-Lyles

Chemistry-Biology

Oxygen radicals and the reactive by-products they create have long been indicated in the disease pathways of metabolic disorders, given that they have the potential to react with the key components of proteins and thus disrupt their functioning. One of the most common by-products of oxygen radicals reacting with components of the cell is 4-hydroxy-2-nonenal (4HNE). Numerous studies have indicated that 4HNE is able to adduct to single amino acids, peptide sequences, as well as whole proteins. Electron transfer flavoprotein (ETF) is a highly active electron transferase of the fatty acid and amino acid oxidation pathways, and deficiency of this protein has been indicated in numerous disease pathways. ETF has demonstrated reduced activity when incubated with 4HNE, therefore this study attempted to determine possible binding sites of 4HNE on ETF by utilizing model peptides and LC-MS analysis. Distinct 4HNE adducts were formed with the peptide angiotensin II as well as a peptide from the alpha subunit of ETF. The groundwork has been laid for further research into the possibility of cross-linking occurring between ETF subunits as well as analysis of 4HNE adducts on ETF through tryptic digest.

Breen-Lyles, Margaret

Senior Showcase Poster presentation

Ripon College

April 19, 2016

The author reserves all rights.

Major: Chemistry-Biology
Minor: Spanish

Summer Research at Ripon College under Dr. Colleen Byron