Radiation Damage to Polypeptides and Proteins in the Solid State: Changes in Amino Acid Composition *

Seredynski, J.; Söylemez, Turan; Baumeister, Wolfgang

doi:10.1515/znc-1981-3-419

Cited by 5 publications

(3 citation statements)

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“…In aspartic and glutamic acids, the formation of a C‐centered radical adjacent to the side‐chain carboxy group is readily observed . Intramolecular radical transfer in 46 under formation of the carboxyl radical 47 leads to a protein‐bound alanyl radical 48 after decarboxylation . The analogous reaction of glutamic acid leads to α‐amino butyric acid …”

Section: Radical Reactions On Proteinsmentioning

confidence: 99%

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The Chemistry of Protein Oxidation in Food

2019

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Oxidation is one of the deterioration reactions of proteins in food, the importance of which is comparable to others such as Maillard, lipation, or protein‐phenol reactions. While research on protein oxidation has led to a precise understanding of the processes and consequences in physiological systems, knowledge about the specific effects of protein oxidation in food or the role of “oxidized” dietary protein for the human body is comparatively scarce. Food protein oxidation can occur during the whole processing axis, from primary production to intestinal digestion. The present review summarizes the current knowledge and mechanisms of food protein oxidation from a chemical, technological, and nutritional–physiological viewpoint and gives a comprehensive classification of the individual reactions. Different analytical approaches are compared, and the relationship between oxidation of food proteins and oxidative stress in vivo is critically evaluated.

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Section: Radical Reactions On Proteinsmentioning

confidence: 99%

“…Intramolecular radical transfer in 46 under formation of the carboxyl radical 47 leads to a protein‐bound alanyl radical 48 after decarboxylation . The analogous reaction of glutamic acid leads to α‐amino butyric acid …”

Section: Radical Reactions On Proteinsmentioning

confidence: 99%

The Chemistry of Protein Oxidation in Food

2019

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“…In Asparagin‐ und Glutaminsäure werden leicht C‐zentrierte Radikale neben der Carboxygruppe in der Seitenkette gebildet . Nach intramolekularem Radikaltransfer im Radikal 46 unter Bildung des Carboxylradikals 47 und folgender Decarboxylierung resultiert ein proteingebundenes Alanylradikal 48 (Schema ) . Die analoge Reaktion der Glutaminsäure führt zu α‐Aminobuttersäure …”

Section: Radikalische Reaktionen An Proteinenunclassified

Die Chemie der Proteinoxidation in Lebensmitteln

Hellwig

2019

Angewandte Chemie

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Die Oxidation ist eine der Abbaureaktionen von Proteinen in Lebensmitteln, deren Bedeutung nicht hinter der von anderen wie der Maillard‐Reaktion, Lipierung oder Protein‐Phenol‐Reaktionen zurückbleibt. Während die Untersuchung der Proteinoxidation zu einem vertieften Verständnis der Prozesse in physiologischen Systemen geführt hat, ist das Wissen über spezifische Auswirkungen der Proteinoxidation in Lebensmitteln oder die Rolle “oxidierter” Lebensmittelproteine für den menschlichen Körper vergleichsweise gering. Oxidationsreaktionen an Lebensmittelproteinen können während des gesamten Verarbeitungsprozesses stattfinden – von der Primärproduktion bis zur Verdauung im Darm. In dem vorliegenden Aufsatz soll das derzeitige Wissen über die Mechanismen der Oxidation von Lebensmittelproteinen aus chemischer, technologischer und ernährungsphysiologischer Sicht zusammengefasst und eine Klassifizierung der einzelnen Reaktionen vorgenommen werden. Verschiedene analytische Ansätze werden verglichen, und der Zusammenhang zwischen der Oxidation von Lebensmittelproteinen und oxidativem Stress in vivo wird kritisch bewertet.

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Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin

Jurasekova¹,

Tinti

Torreggiani

2011

Anal Bioanal Chem

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Damages induced by free radicals on human serum albumin (HSA), the most prominent protein in plasma, were investigated by Raman spectroscopy. HSA underwent oxidative and reductive radical stress. Gamma-irradiation was used to simulate the endogenous formation of reactive radical species such as hydrogen atoms ((•)H), solvated electrons (e(aq)(-)) and hydroxyl radicals ((•)OH). Raman spectroscopy was shown to be a useful tool in identifying conformational changes of the protein structure and specific damages occurring at sensitive amino acid sites. In particular, the analysis of the S-S stretching region suggested the radical species caused modifications in the 17 disulphide bridges of HSA. The concomitant action of e(aq)(-) and (•)H atoms caused the formation of cyclic disulphide bridges, showing how cystine pairs act as efficient interceptors of reducing species, by direct scavenging and electron transfer reactions within the protein. This conclusion was further confirmed by the modifications visible in the Raman bands due to Phe and Tyr residues. As regards to protein folding, both oxidative and reductive radical stresses were able to cause a loss in α-helix content, although the latter remains the most abundant secondary structure component. β-turns motifs significantly increased as a consequence of the synergic action of e(aq)(-) and (•)H atoms, whereas a larger increase in the β-sheet content was found following the exposure to (•)OH and/or (•)H attack.

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Radiation Damage to Polypeptides and Proteins in the Solid State: Changes in Amino Acid Composition *

Cited by 5 publications

References 0 publications

The Chemistry of Protein Oxidation in Food

The Chemistry of Protein Oxidation in Food

Die Chemie der Proteinoxidation in Lebensmitteln

Use of Raman spectroscopy for the identification of radical-mediated damages in human serum albumin

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