Mass Spectrometry: Structure Determination of Proteins and Peptides

Dass, Chhabil

doi:10.1016/b978-008045382-8.00685-7

Cited by 3 publications

(7 citation statements)

References 170 publications

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“…MS-MS is the leading technique for the determination of peptides and other biomolecules [ 106 ], is used to quantitatively and qualitatively study arsenosugars [ 84 , 107 ] and phlorotannins from seaweeds [ 84 ].…”

Section: Identification Characterization and Quantification Of The Bioactive Compounds From Seaweeds Extractsmentioning

confidence: 99%

Marine Health-Promoting Compounds: Recent Trends for Their Characterization and Human Applications

Quitério

Soares

Ferraz

et al. 2021

Foods

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Seaweeds represent a rich source of biologically active compounds with several applications, especially in the food, cosmetics, and medical fields. The beneficial effects of marine compounds on health have been increasingly explored, making them an excellent choice for the design of functional foods. When studying marine compounds, several aspects must be considered: extraction, identification and quantification methods, purification steps, and processes to increase their stability. Advanced green techniques have been used to extract these valuable compounds, and chromatographic methods have been developed to identify and quantify them. However, apart from the beneficial effects of seaweeds for human health, these natural sources of bioactive compounds can also accumulate undesirable toxic elements with potential health risks. Applying purification techniques of extracts from seaweeds may mitigate the amount of excessive toxic components, ensuring healthy and safer products for commercialization. Furthermore, limitations such as stability and bioavailability problems, chemical degradation reactions during storage, and sensitivity to oxidation and photo-oxidation, need to be overcome using, for example, nanoencapsulation techniques. Here we summarize recent advances in all steps of marine products identification and purification and highlight selected human applications, including food and feed applications, cosmetic, human health, and fertilizers, among others.

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Section: Identification Characterization and Quantification Of The Bioactive Compounds From Seaweeds Extractsmentioning

confidence: 99%

Marine Health-Promoting Compounds: Recent Trends for Their Characterization and Human Applications

Quitério

Soares

Ferraz

et al. 2021

Foods

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“…The most frequently used approach is to submit the peptide to CID-MS/MS analysis. According to our current knowledge of fragmentation of non-phosphopeptide ions (Dass, 2000(Dass, , 2007(Dass, , 2009a(Dass, , 2009b, the b and y sequence-specific ions also dominate the CID spectra of phosphopeptides. The residue masses of phosphoserine, phosphothreonine, and phosphotyrosine are shifted to 167, 181, and 243 Da, respectively.…”

Section: Collision-induced Dissociation Ms/msmentioning

confidence: 98%

“…Currently, it has become feasible to analyze proteins and in particular phosphoproteins on a large-scale using proteomic approach (Collins et al, 2007;Dass, 2007Dass, , 2009aParadela and Albar, 2008;Reinders and Sickmann, 2005;Rossignol, 2006;Salih, 2005;Temporini et al, 2008;Zahedi et al, 2006). A general protocol for mass spectrometricbased phosphoproteomics is illustrated in Fig.…”

Section: Mass Spectrometry and Phosphopro-teomicsmentioning

confidence: 99%

“…*Address correspondence to this author at the Department of Chemistry, JM Smith Building, The University of Memphis, Memphis, TN 38152, USA;Tel: 901-678-2628;Fax: 901-678-3447;E-mail: cdass@memphis.edu Understanding of the highly interconnected regulatory network requires identifying, cataloging, and quantitating protein phosphorylation. Mass spectrometry-driven current protocols of phosphoproteomics are becoming highly valuable in achieving these objectives (Dass, 2000(Dass, , 20072009a). Phosphoproteomics is a sub-field of proteomics that deals with comprehensive analysis of phosphoproteome-the entire complement of phosphoproteins in biological systems, including detection of all phosphoproteins, location of the exact site of phosphorylation, and quantification of differentially expressed phosphoproteins.…”

Section: Introductionmentioning

confidence: 99%

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Recent Developments in Mass Spectrometry Analysis of Phosphoproteomes

Dass¹

2009

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Phosphorylation is one of the most important and ubiquitous modifications in eukaryotic cells. This covalent modification is a major signaling pathway in living beings. A vast array of cellular events, such as proliferation, differentiation, metabolism, signal transduction, and adaptation to environmental stress, and the function of many proteins, hormones, neurotransmitters, and enzymes, are triggered by phosphorylation. For understanding highly interconnected regulatory network, it is essential to identify and quantify phosphoproteins in biological specimens. Currently, this task is accomplished by mass spectrometry-driven phosphoproteomics. This article outlines recent developments in the analysis of phosphoproteins, specifically, the enrichment, detection, identification, and quantification of phosphopeptides/phosphoproteins.

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“…There are several types of MS/MS fragmentation processes, such as electron-transfer dissociation (ETD), electron-capture dissociation (ECD), and collision-induced dissociation (CID) [60]. A common and straightforward mechanism to implement the process is CID, which employs collisions of the fast-moving peptide ions with neutral inert gas [61]. Hence, in tandem MS, at first, the peptides are separated by MS spectrum, and then specific peptides with particular mass are selected for collision-induced dissociation (CID) in a collision cell.…”

Section: Sample Analysis and Data Acquisition In Biomarker Developmentmentioning

confidence: 99%

Proteomics techniques in protein biomarker discovery

Babaei,

Kashanian,

Lee

et al. 2024

Quant. Biol.

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Protein biomarkers represent specific biological activities and processes, so they have had a critical role in cancer diagnosis and medical care for more than 50 years. With the recent improvement in proteomics technologies, thousands of protein biomarker candidates have been developed for diverse disease states. Studies have used different types of samples for proteomics diagnosis. Samples were pretreated with appropriate techniques to increase the selectivity and sensitivity of the downstream analysis and purified to remove the contaminants. The purified samples were analyzed by several principal proteomics techniques to identify the specific protein. In this study, recent improvements in protein biomarker discovery, verification, and validation are investigated. Furthermore, the advantages, and disadvantages of conventional techniques, are discussed. Studies have used mass spectroscopy (MS) as a critical technique in the identification and quantification of candidate biomarkers. Nevertheless, after protein biomarker discovery, verification and validation have been required to reduce the false‐positive rate where there have been higher number of samples. Multiple reaction monitoring (MRM), parallel reaction monitoring (PRM), and selected reaction monitoring (SRM), in combination with stable isotope‐labeled internal standards, have been examined as options for biomarker verification, and enzyme‐linked immunosorbent assay (ELISA) for validation.

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Mass Spectrometry: Structure Determination of Proteins and Peptides

Cited by 3 publications

References 170 publications

Marine Health-Promoting Compounds: Recent Trends for Their Characterization and Human Applications

Marine Health-Promoting Compounds: Recent Trends for Their Characterization and Human Applications

Recent Developments in Mass Spectrometry Analysis of Phosphoproteomes

Proteomics techniques in protein biomarker discovery

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