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Identification And Quantification Of Oxidative Modification Of Peptides And Proteins By Mass Spectrometry
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Book Synopsis Identification and Quantification of Oxidative Modification of Peptides and Proteins by Mass Spectrometry by : Lijie Men
Download or read book Identification and Quantification of Oxidative Modification of Peptides and Proteins by Mass Spectrometry written by Lijie Men and published by . This book was released on 2007 with total page 360 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Mass Spectrometry of Proteins and Peptides by : John R. Chapman
Download or read book Mass Spectrometry of Proteins and Peptides written by John R. Chapman and published by Springer Science & Business Media. This book was released on 2008-02-05 with total page 539 pages. Available in PDF, EPUB and Kindle. Book excerpt: Little more than three years down the line and I am already writing the Preface to a second volume to follow Protein and Peptide Analysis by Mass . What has happened in between these times to make this second venture worthwhile? New types of mass spectrometric instrumentation have appeared so that new techniques have become possible and existing techniques have become much more feasible. More particularly, however, the newer ionization te- niques, introduced for the analysis of high molecular weight materials, have now been thoroughly used and studied. As a result, there has been an en- mous improvement in the associated sample handling technology so that these methods are now routinely applied to much smaller sample amounts as well as to more intractable samples. Again, this particular community of mass spectrometry users has both increased in number and diversified. And, riding this wave of acceptance, leaders in the field have set their sights on more complex problems: molecular interaction, ion structures, quantitation, and kinetics are just a few of the newer areas reported in Mass Spectrometry of Proteins and Peptides. As with the first volume, one purpose of this collection, Mass Spectr- etry of Proteins and Peptides, is to show the reader what can be done by the application of mass spectrometry, and perhaps even to encourage the reader to venture down new paths.
Download or read book Neuroproteomics written by Oscar Alzate and published by CRC Press. This book was released on 2009-10-26 with total page 356 pages. Available in PDF, EPUB and Kindle. Book excerpt: In this, the post-genomic age, our knowledge of biological systems continues to expand and progress. As the research becomes more focused, so too does the data. Genomic research progresses to proteomics and brings us to a deeper understanding of the behavior and function of protein clusters. And now proteomics gives way to neuroproteomics as we beg
Book Synopsis Mass Spectrometry-based Identification and Characterization of Protein and Peptide Adducts of Lipoxidation-derived Aldehydes by : Juan D. Chavez
Download or read book Mass Spectrometry-based Identification and Characterization of Protein and Peptide Adducts of Lipoxidation-derived Aldehydes written by Juan D. Chavez and published by . This book was released on 2010 with total page 702 pages. Available in PDF, EPUB and Kindle. Book excerpt: Oxidative stress is recognized as an important underlying factor in the pathogenesis of many degenerative diseases as well as normal senescence. The free radicals, reactive oxygen species (ROS) and electrophiles produced during oxidative stress are capable of modifying nucleic acids, lipids and proteins. There are a variety of oxidative modifications that occur to proteins including: cleavage of the protein backbone, direct oxidation of amino acid side chains by ROS, and adduction by electrophilic species such as lipid peroxidation products. Many of these oxidative modifications result in the introduction of carbonyl groups into the proteins. Protein carbonylation levels are commonly used as a biomarker to assess the degree of oxidative damage to a system. However the most commonly employed methods for measuring oxidative modifications to proteins, typically fail to provide any information about the identity of the modified protein, site of modification, or the chemical nature of the modification. In the present study we develop an analytical technique based on affinity labeling with N'-aminooxymethylcarbonylhydrazino-D-biotin (aldehyde reactive probe, ARP), along with mass spectrometric analysis which allows for the full characterization of protein carbonylation modifications. The ability of the ARP method was first demonstrated for the case of oxylipid peptide and protein conjugates formed by Michael addition-type conjugation reactions with [alpha,beta]- unsaturated aldehydic lipid peroxidation products with nucleophilic amino acid residue side chains. ARP was used to label a 4-hydroxy-2-nonenal (HNE) modified cysteine containing model peptide, and HNE modified E. coli thioredoxin, which were characterized using ESI-MS/MS and MALDI-MS/MS. ARP was also used to label the oxidative modifications alpha-aminoadipic semialdehyde (AAS) and gamma-glutamic semialdehyde (GGS), formed during the metal catalyzed oxidation of GAPDH. After demonstrating the utility of the technique on model systems, it was then applied to complex biological systems. In one case, subsarcolemmal mitochondria (SSM) isolated from rat cardiac tissue. Mitochondria are well known to be a major source of ROS within the cell. They are therefore important mediators of oxidative stress, as well as regulators of cell death. We were able to identify 39 unique sites on 27 mitochondrial proteins which were modified by six different [alpha,beta]-unsaturated aldehydes, including acrolein, [beta]-hydroxyacrolein, crotonaldehyde, 4-hydroxy-2-hexenal, 4-hydroxy-2-nonenal and 4-oxo-2- nonenal. Additionally we identified nine Lys residues on four mitochondrial proteins that were oxidized to AAS and subsequently labeled with ARP. The proteins identified with oxidative modifications include members of the mitochondrial electron transport chain, TCA cycle, membrane transport, lipid metabolism, and other important mitochondrial enzymes. The ARP technique was also applied to identify protein targets of 4-hyroxy-2- nonenal in human monocytic THP-1 cells that were exogenously exposed to HNE. It was shown previously that exposure of THP-1 cells to HNE resulted in apoptosis, necrosis and protein carbonylation. We applied a multi-pronged proteomic approach involving electrophoretic, immunoblotting and mass spectrometric analysis to unequivocally identify eighteen sites of HNE modification on sixteen proteins. It was also demonstrated in this study that pretreatment of THP-1 cells with ascorbic acid resulted in decreased levels of HNE-protein conjugate formation.
Book Synopsis Analysis of Protein Post-Translational Modifications by Mass Spectrometry by : John R. Griffiths
Download or read book Analysis of Protein Post-Translational Modifications by Mass Spectrometry written by John R. Griffiths and published by John Wiley & Sons. This book was released on 2016-11-07 with total page 414 pages. Available in PDF, EPUB and Kindle. Book excerpt: Covers all major modifications, including phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation Discussion of the chemistry behind each modification, along with key methods and references Contributions from some of the leading researchers in the field A valuable reference source for all laboratories undertaking proteomics, mass spectrometry and post-translational modification research
Book Synopsis Multistage Tandem Mass Spectrometry Strategies for the Targeted Analysis of Oxidative Protein Modifications by : Jennifer M. Froelich
Download or read book Multistage Tandem Mass Spectrometry Strategies for the Targeted Analysis of Oxidative Protein Modifications written by Jennifer M. Froelich and published by . This book was released on 2008 with total page 460 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Author :Willy Vincent Bienvenut Publisher :Springer Science & Business Media ISBN 13 :9781402033186 Total Pages :324 pages Book Rating :4.0/5 (331 download)
Book Synopsis Acceleration and Improvement of Protein Identification by Mass Spectrometry by : Willy Vincent Bienvenut
Download or read book Acceleration and Improvement of Protein Identification by Mass Spectrometry written by Willy Vincent Bienvenut and published by Springer Science & Business Media. This book was released on 2005-04-19 with total page 324 pages. Available in PDF, EPUB and Kindle. Book excerpt: At present where protein identification and characterisation using mass spectrometry is a method of choice, this book is presenting a review of basic proteomic techniques. The second part of the book is related to the novel high throughput protein identification technique called the 'molecular scanner'. Several protein identification techniques are described, especially the peptide mass fingerprint with MALDI-MS based method. E.g. ionisation process, matrix available, signal reproducibility and suppression effect, as well as date treatment for protein identification using bioinformatics tools.
Book Synopsis Mass Spectrometry: Modified Proteins and Glycoconjugates by : A.L. Burlingame
Download or read book Mass Spectrometry: Modified Proteins and Glycoconjugates written by A.L. Burlingame and published by Gulf Professional Publishing. This book was released on 2005-12-13 with total page 482 pages. Available in PDF, EPUB and Kindle. Book excerpt: This volume provides comprehensive treatment of tools and proper usage for the identification of proteins, affinity chromatography and studies the complexity of protein machines and assemblages, assignment of the most common protein posttranslational modifications (phosphorylation and glycosylation) and glycolipidomics. *Part 2 of 2 volumes about Mass Spectrometry *Discusses peptide and protein cleanup and preparation requirements for mass spectrometry *Explains protein enzymic and chemical digestion strategies *Includes case studies of protein assemblages and machines
Book Synopsis Protein and Peptide Mass Spectrometry in Drug Discovery by : Michael L. Gross
Download or read book Protein and Peptide Mass Spectrometry in Drug Discovery written by Michael L. Gross and published by John Wiley & Sons. This book was released on 2011-09-26 with total page 484 pages. Available in PDF, EPUB and Kindle. Book excerpt: The book that highlights mass spectrometry and its application in characterizing proteins and peptides in drug discovery An instrumental analytical method for quantifying the mass and characterization of various samples from small molecules to large proteins, mass spectrometry (MS) has become one of the most widely used techniques for studying proteins and peptides over the last decade. Bringing together the work of experts in academia and industry, Protein and Peptide Mass Spectrometry in Drug Discovery highlights current analytical approaches, industry practices, and modern strategies for the characterization of both peptides and proteins in drug discovery. Illustrating the critical role MS technology plays in characterizing target proteins and protein products, the methods used, ion mobility, and the use of microwave radiation to speed proteolysis, the book also covers important emerging applications for neuroproteomics and antigenic peptides. Placing an emphasis on the pharmaceutical industry, the book stresses practice and applications, presenting real-world examples covering the most recent advances in mass spectrometry, and providing an invaluable resource for pharmaceutical scientists in industry and academia, analytical and bioanalytical chemists, and researchers in protein science and proteomics.
Book Synopsis Mass Spectrometry-Based Chemical Proteomics by : W. Andy Tao
Download or read book Mass Spectrometry-Based Chemical Proteomics written by W. Andy Tao and published by John Wiley & Sons. This book was released on 2019-07-10 with total page 448 pages. Available in PDF, EPUB and Kindle. Book excerpt: PROVIDES STRATEGIES AND CONCEPTS FOR UNDERSTANDING CHEMICAL PROTEOMICS, AND ANALYZING PROTEIN FUNCTIONS, MODIFICATIONS, AND INTERACTIONS—EMPHASIZING MASS SPECTROMETRY THROUGHOUT Covering mass spectrometry for chemical proteomics, this book helps readers understand analytical strategies behind protein functions, their modifications and interactions, and applications in drug discovery. It provides a basic overview and presents concepts in chemical proteomics through three angles: Strategies, Technical Advances, and Applications. Chapters cover those many technical advances and applications in drug discovery, from target identification to validation and potential treatments. The first section of Mass Spectrometry-Based Chemical Proteomics starts by reviewing basic methods and recent advances in mass spectrometry for proteomics, including shotgun proteomics, quantitative proteomics, and data analyses. The next section covers a variety of techniques and strategies coupling chemical probes to MS-based proteomics to provide functional insights into the proteome. In the last section, it focuses on using chemical strategies to study protein post-translational modifications and high-order structures. Summarizes chemical proteomics, up-to-date concepts, analysis, and target validation Covers fundamentals and strategies, including the profiling of enzyme activities and protein-drug interactions Explains technical advances in the field and describes on shotgun proteomics, quantitative proteomics, and corresponding methods of software and database usage for proteomics Includes a wide variety of applications in drug discovery, from kinase inhibitors and intracellular drug targets to the chemoproteomics analysis of natural products Addresses an important tool in small molecule drug discovery, appealing to both academia and the pharmaceutical industry Mass Spectrometry-Based Chemical Proteomics is an excellent source of information for readers in both academia and industry in a variety of fields, including pharmaceutical sciences, drug discovery, molecular biology, bioinformatics, and analytical sciences.
Book Synopsis Improvements to the Identification and Quantification of Peptides and Proteins by : Christopher Michael Rose
Download or read book Improvements to the Identification and Quantification of Peptides and Proteins written by Christopher Michael Rose and published by . This book was released on 2014 with total page 294 pages. Available in PDF, EPUB and Kindle. Book excerpt: The following chapters contain a plethora of proteomic techniques aimed at the improvement of methods for the identification and quantification of peptide and protein species. The genesis of mass spectrometry for the analysis of biological molecules and the advances that have resulted in the large-scale identification and quantification of proteins are detailed in Chapter 1. Chapter 2 discusses the application of quantitative proteomic techniques for the large-scale analysis of a biological system, Medicago truncatula. The third chapter discusses the implementation of an online algorithm to identify peptides in real time (InSeq), enabling alterations to the instrument method that increase the quantitative accuracy of measurements or aid in post translational modification localization. Chapters 4 to 6 outline advances to the implementation of electron transfer dissociation aimed at increasing the ability to identify protein (Chapter 4) or peptide (Chapters 5 and 6) species. The remainder of this thesis details the application of neutron encoded (NeuCode) mass labels to peptide identification without tandem MS (Chapter 7), top-down quantification of intact proteoforms (Chapter 8), labeling of mammals that enables multiplexed quantitative analysis of mammalian tissue after only 10 days of labeling time (Chapter 9), and targeted quantification of more than 1,000 peptides (Chapter 10). Conclusions and future directions relating to the content of this thesis are discussed in Chapter 11.
Book Synopsis Identification and Quantification of the Post-translational Modifications of Nucleosomal Proteins Using Mass Spectrometry by : Xinzhao Jiang
Download or read book Identification and Quantification of the Post-translational Modifications of Nucleosomal Proteins Using Mass Spectrometry written by Xinzhao Jiang and published by . This book was released on 2006 with total page 454 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Harnessing Radical Chemistry for the Facile Identification of Post Translational Modification Sites in Proteins by Photodissociation Mass Spectrometry by : Jolene Katie Diedrich
Download or read book Harnessing Radical Chemistry for the Facile Identification of Post Translational Modification Sites in Proteins by Photodissociation Mass Spectrometry written by Jolene Katie Diedrich and published by . This book was released on 2011 with total page 141 pages. Available in PDF, EPUB and Kindle. Book excerpt: Also reported is the discovery of photodissociation at 266 nm to selectively cleave disulfide bonds in the gas phase, while leaving all other bonds intact. This methodology can be used to identify disulfide bonded pairs in complex systems. LC-MS experiments utilizing photodissociation were developed for analysis of protein digests. Peptides containing biomarkers of oxidative stress can be easily identified by LC-PD-MS. Proteins exposed to oxidative stress can be halogenated at tyrosine residues. Homolytic cleavage of the carbon-halogen bond is a favorable process and allows facile identification of these types of biomarkers. Shown in this dissertation is the selectivity offered by photodissociation; homolytic cleavage allows simplification of data analysis by quickly identifying the peptides of interest in a mixture while subsequent selective backbone fragmentation allows facile analysis of protein modifications.
Book Synopsis Protein Analysis using Mass Spectrometry by : Mike S. Lee
Download or read book Protein Analysis using Mass Spectrometry written by Mike S. Lee and published by John Wiley & Sons. This book was released on 2017-06-19 with total page 290 pages. Available in PDF, EPUB and Kindle. Book excerpt: Presents Practical Applications of Mass Spectrometry for Protein Analysis and Covers Their Impact on Accelerating Drug Discovery and Development Covers both qualitative and quantitative aspects of Mass Spectrometry protein analysis in drug discovery Principles, Instrumentation, Technologies topics include MS of peptides, proteins, and ADCs , instrumentation in protein analysis, nanospray technology in MS protein analysis, and automation in MS protein analysis Details emerging areas from drug monitoring to patient care such as Identification and validation of biomarkers for cancer, targeted MS approaches for biomarker validation, biomarker discovery, and regulatory perspectives Brings together the most current advances in the mass spectrometry technology and related method in protein analysis
Book Synopsis Tandem Mass Spectrometric Analysis of Protein and Peptide Adducts of Lipid Peroxidation-derived Aldehydes by : Jianyong Wu
Download or read book Tandem Mass Spectrometric Analysis of Protein and Peptide Adducts of Lipid Peroxidation-derived Aldehydes written by Jianyong Wu and published by . This book was released on 2010 with total page 434 pages. Available in PDF, EPUB and Kindle. Book excerpt: The adduction of proteins and other biomolecules by electrophilic lipid peroxidation products such as 4-hydroxy-2-nonenal (HNE), 4-oxo-2-nonenal (ONE), malondialdehyde (MDA) or acrolein (ACR) is thought to be an initiating and/or propagating factor in the pathophysiology of several diseases such as atherosclerosis, diabetes, Alzheimer's, Parkinson's and other age-related disorders. The identification of protein sites modified by oxylipids is of key relevance for advancing our understanding how oxidative damage affects structure and function of proteins. Here, the use of MALDI tandem mass spectrometry with high energy collision-induced dissociation (CID) on a TOF/TOF instrument for sequencing oxylipid-peptide conjugates was systematically studied. Three synthesized model peptides containing one nucleophilic residue (i.e. Cys, His or Lys) were reacted with MDA, HNE, ONE and ACR. MALDI-MS analysis and MS/MS analysis were performed to confirm the adduct type and the modification sites. Michael adducts and Schiff bases were the predominant products under pH 7.4 within 2 hours. All MS/MS spectra of Michael adducts show the neutral loss of the oxylipid moiety ions. MS/MS spectra of Cys-containing peptide oxylipid conjugates exhibit additional characteristic neutral loss of HS-oxylipid moiety ions. MS/MS spectra of His-containing peptide oxylipid conjugates show characteristic oxylipid-containing His immonium ions. Spectra of Lys-containing peptide oxylipid conjugates (Schiff base) also show oxylipid-containing Lys immonium ions. However, there is no neutral loss of the oxylipid moiety ion for these Schiff bases. Determining the extent or relative amounts of the oxidative damage in cells could provide valuable insights into the molecular mechanisms of the diseases caused by oxidative stress. Relative quantitation of oxylipid-modified proteins in biological samples is a challenging problem because of the complexity and extreme dynamic range that characterize these samples. In this study, the reagents, N'-aminooxymethylcarbonylhydrazino-D-biotin (ARP) and iodoacetyl-PEO2- biotin (IPB), were used to enrich acrolein-modified Cys-containing peptides and the corresponding unmodified ones from subsarcolemmal mitochondria (SSM). The ratios between them were determined by nanoLC-SRM analysis. Model Cys-containing peptides labeled with ARP-acrolein and IPB were employed to demonstrate this method. Seven acrolein-modifed Cys-containing peptides from five mitochondrial proteins were quantified. The ratios for those seven peptides from the CCl4-treated rats are higher than the control ones indicating that the ratios of acrolein-modified peptides to unmodified ones are potential markers of oxidative stress in vivo. Age-dependent changes of protein carbonyls were investigated in subsarcolemmal mitochondria by using LC-SRM analysis of distinct ACR-modified Cys-containing peptides. Immunochemical analysis using an anti-ACR monoclonal antibody supported an increase of proteins modified by acrolein with age. However, total protein carbonyls measurement using ARP in Western blot analysis did not conform to this change suggesting that age-related changes in protein carbonyls are complex and would benefit from more specific measurement protocols.
Book Synopsis Mass Spectroscopic Identification and Quantification of Protein Carbonyls by : Zafer Ugur
Download or read book Mass Spectroscopic Identification and Quantification of Protein Carbonyls written by Zafer Ugur and published by . This book was released on 2012 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: It is well established that free radical mediated oxidative stress plays a critical role in aging and age-related diseases. Among the post-translational protein modifications, carbonylation has attracted a great deal of attention due to its irreversible and irreparable nature. Despite the fact that protein carbonylation is associated with a series of physiological and pathological processes, there are still issues to be clarified such as why certain proteins are more vulnerable to modification, what are the locations of the protein modifications, and how does the nature of the oxidant affect the preferred site of modification. In this study, we will seek an answer to these questions and examine the global effect of oxidative stress on protein abundance. The study embraces three distinct specific aims. In the first, methods are developed for identifying sites of protein carbonylation. In the second specific aim, these methods are used to identify carbonylation sites in model proteins subjected to chemical oxidants. In the third aim, the focus is on a model organism, C. elegans, subjected to paraquat-induced oxidative stress. This is exploratory work and mass spectrometry is used to assess the impact of oxidative stress on the mitochondrial proteome.
Book Synopsis Identification and Quantification of Protein Carbonylation by Mass Spectrometry by : Qingyuan Liu
Download or read book Identification and Quantification of Protein Carbonylation by Mass Spectrometry written by Qingyuan Liu and published by . This book was released on 2012 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Accumulated evidence indicates oxidative stress plays important roles in disease and aging. Under oxidative stress, lipid peroxidation (LPO) leads to reactive carbonyl species (RCS) that can modify a wide range of biomolecules including protein, DNA and carbohydrate. In this dissertation, we investigate the modification of two model proteins, human serum albumin (HSA) and aconitase (ACO), by the LPO-relevant a, b-unsaturated aldehydes, acrolein (ACR) and 4-hydroxy-2-nonenal (HNE). The investigation is focused on the characterization and quantification ACR and HNE addition to the model proteins. A correlation between HNE modification and ACO activity is also determined. These results provide insights into the impact of oxidative stress at the molecular level and are relevant to aging and disease states. We finally investigate protein carbonylation in ischemic mouse heart mitochondria, and develop a quantitative method for detecting carbonylated protein in this system. The research is based on liquid chromatography/mass spectrometry (LC/M.S.), Western Blots, and enzymatic assay.
