Mass Spectrometric Strategies for Identification and Characterization of Carbonylated Peptides and Proteins

Carini, Marina; Orioli, Marica

doi:10.1002/9780813814438.ch11

Cited by 4 publications

(3 citation statements)

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“…Likely CSF-borne molecules include 4-hydroxynonenal, acrolein, and malondialdehyde, all of which are highly reactive aldehyde products of ROS-catalyzed lipid peroxidation. Unlike ROS, however, these compounds are relatively long-lived and can withstand extracellular transport from their site of generation [22,31]. In this regard, elevated levels of 4-hydroxynonenal have been documented in the CSF of patients with neuropathologies, including amyotrophic lateral sclerosis [32] and Parkinson's disease [33].…”

Section: Discussionmentioning

confidence: 99%

Protein carbonylation after traumatic brain injury: cell specificity, regional susceptibility, and gender differences

Lazarus

Buonora

Jacobowitz

et al. 2015

Free Radical Biology and Medicine

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Protein carbonylation is a well-documented and quantifiable consequence of oxidative stress in several neuropathologies, including multiple sclerosis, Alzheimer׳s disease, and Parkinson׳s disease. Although oxidative stress is a hallmark of traumatic brain injury (TBI), little work has explored the specific neural regions and cell types in which protein carbonylation occurs. Furthermore, the effect of gender on protein carbonylation after TBI has not been studied. The present investigation was designed to determine the regional and cell specificity of TBI-induced protein carbonylation and how this response to injury is affected by gender. Immunohistochemistry was used to visualize protein carbonylation in the brains of adult male and female Sprague-Dawley rats subjected to controlled cortical impact (CCI) as an injury model of TBI. Cell-specific markers were used to colocalize the presence of carbonylated proteins in specific cell types, including astrocytes, neurons, microglia, and oligodendrocytes. Results also indicated that the injury lesion site, ventral portion of the dorsal third ventricle, and ventricular lining above the median eminence showed dramatic increases in protein carbonylation after injury. Specifically, astrocytes and limited regions of ependymal cells adjacent to the dorsal third ventricle and the median eminence were most susceptible to postinjury protein carbonylation. However, these patterns of differential susceptibility to protein carbonylation were gender dependent, with males showing significantly greater protein carbonylation at sites distant from the lesion. Proteomic analyses were also conducted and determined that the proteins most affected by carbonylation in response to TBI include glial fibrillary acidic protein, dihydropyrimidase-related protein 2, fructose-bisphosphate aldolase C, and fructose-bisphosphate aldolase A. Many other proteins, however, were not carbonylated by CCI. These findings indicate that there is both regional and protein specificity in protein carbonylation after TBI. The marked increase in carbonylation seen in ependymal layers distant from the lesion suggests a mechanism involving the transmission of a cerebral spinal fluid-borne factor to these sites. Furthermore, this process is affected by gender, suggesting that hormonal mechanisms may serve a protective role against oxidative stress.

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Section: Discussionmentioning

confidence: 99%

Protein carbonylation after traumatic brain injury: cell specificity, regional susceptibility, and gender differences

Lazarus

Buonora

Jacobowitz

et al. 2015

Free Radical Biology and Medicine

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“…Less reactive side chains include indole groups (i.e., tryptophan side chains), amide groups (i.e., asparagine and glutamine side chains), imidazole groups (i.e., histidine side chains), and the phenolic side chain of tyrosine . Some of this work has focused on how these reactions alter the structure or functional properties of proteins, e.g., changes in their emulsifying, foaming, or other properties. − , …”

Section: Introductionmentioning

confidence: 99%

“…10 Some of this work has focused on how these reactions alter the structure or functional properties of proteins, e.g., changes in their emulsifying, foaming, or other properties. [10][11][12]15 Using ultra-high-pressure liquid chromatography with electrospray ionization coupled with quadrupole time-of-flight MS (UPLC−ESI−QTOF−MS), we have reported on covalent reactions that occur between the protein β-lactoglobulin (BLG) and a broad range of flavor molecules under storage at ambient temperatures 16,17 and in various reaction environ-ments 18 (pH and water activity). For example, reaction rates have been observed to be lower at pH 3 and higher at pH 7 or pH 8.…”

Section: ■ Introductionmentioning

confidence: 99%

Covalent Adduct Formation between β-Lactoglobulin and Flavor Compounds under Thermal Treatments That Mimic Food Pasteurization or Sterilization

Yuan

Anantharamkrishnan

Hoye

et al. 2023

J. Agric. Food Chem.

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Thermal processing (e.g., pasteurization and sterilization) is a critical step ensuring the microbial safety of our foods. Previous work from our laboratory has examined the covalent reactions occurring between proteins and a broad selection of flavor compounds under ambient storage temperatures (25−45 °C). However, similar research on reactions of flavor compounds with a protein under thermal processing conditions has not been investigated. In the current study, covalent adduct formation between βlactoglobulin (BLG) and 46 flavor compounds encompassing 13 different classes of functional groups was investigated under pasteurization and sterilization conditions by UPLC−ESI−QTOF−MS. BLG was chosen as a representative protein for this study because it is structurally well characterized, its molecular weight is well suited for ESI−MS analysis (18.2 kDa), and it is broadly used in the food industry. Schiff base, aza-Michael addition, and disulfide linkages were the main types of covalent interactions occurring across the reactive samples. Among them, isothiocyanates, aldehydes, and thiol-containing compounds were generally very reactive. Increasing the severity of the thermal treatment [high-temperature-short-time (HTST) pasteurization, in-container pasteurization (IC), and ultra-high-temperature (UHT) sterilization conditions] accelerated the reactions of BLG with flavor compounds, which revealed reactivity of three flavor compounds not previously observed to react at room temperature (eugenol, 4-vinyl phenol, and 3nonen-2-one). Ketones [other than 2-hydroxy-3-methyl-2-cyclopenten-1-one (cyclotene), diketones, and unsaturated ketones], alcohols, acids, alkenes (terpenes), esters, lactones, 3-acetylpyridine, methyl anthranilate, vanillin, 2-methylthiophene, and dimethyl sulfone did not show measurable reactivity with BLG under the thermal processing conditions examined. An overall view of the data shows that the HTST heat treatment (72 °C for 15 s) had the least effect on the extent of reaction while in-container pasteurization conditions (63 °C for 30 min) produced a similar extent of reaction as the UHT (130 °C 30 s) heat treatment. These varying extents of adductation are in reasonable accord with what one might expect, given that the rates of most classes of chemical reactions occurring near ambient temperature increase by a factor of 2−4 for each increase of 10 K in temperature. Unfortunately, our methodology did not permit us to obtain meaningful data using the most aggressive standard sterilization thermal conditions (110 °C for 30 min) because extensive aggregation/coagulation removed essentially all of the BLG protein from the reaction mixtures prior to MS analysis.

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Chemical and Instrumental Characterization of Protein–Flavor Interactions

Anantharamkrishnan,

Reineccius

2023

Flavour and Consumer Perception of Food Proteins

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In all fields of science, the ability to advance understanding and knowledge is tied to the ability to measure outcomes. As early as 1920, it was observed that the composition of a food influences the sensory perception of aroma compounds added to it. However, it was not until the early 1960s that gas chromatographic instrumentation became available to measure how and what was responsible for influencing flavor perception as the food composition was altered. The early methods were fairly simple, depending on headspace analysis to gain an understanding. Headspace methodologies lacked sensitivity to work in the range of human perception on many aroma compounds, and thus, more sensitive methods were developed, such as equilibrium dialysis and headspace concentration techniques. The most recent developments in this area employ sophisticated mass spectrometry to measure how flavor compounds react with food proteins and where they react within the protein. This chapter tracks the development of methodology and learning focusing on both weak (ionic, hydrophilic, and hydrophobic) and strong (covalent) bonding of flavor compounds to various protein sources.

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Mass Spectrometric Strategies for Identification and Characterization of Carbonylated Peptides and Proteins

Cited by 4 publications

References 104 publications

Protein carbonylation after traumatic brain injury: cell specificity, regional susceptibility, and gender differences

Protein carbonylation after traumatic brain injury: cell specificity, regional susceptibility, and gender differences

Covalent Adduct Formation between β-Lactoglobulin and Flavor Compounds under Thermal Treatments That Mimic Food Pasteurization or Sterilization

Chemical and Instrumental Characterization of Protein–Flavor Interactions

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