The effect of neighboring amino acid residues and solution environment on the oxidative stability of tyrosine in small peptides

Zhang, Jian; Kalonia, Devendra S.

doi:10.1208/pt0804102

Cited by 17 publications

(10 citation statements)

References 30 publications

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“…The mechanism leading to the anti-oxidative effects of negatively charged species remains unclear. A recent study (Zhang and Kalonia, 2007) reports that the degree of oxidation of tyrosine and tyrosyl peptides is reduced in the presence of adjacent negatively charged amino acids, supporting the anti-oxidative effect of negative surface charges. However, the exact mechanism needs to be investigated further.…”

Section: Discussionmentioning

confidence: 89%

Synthetic polymeric substrates as potent pro‐oxidant versus anti‐oxidant regulators of cytoskeletal remodeling and cell apoptosis

Sung¹,

Chandra²,

Treiser³

et al. 2008

Journal Cellular Physiology

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The role of reactive oxygen species (ROS)-mediated cell signal transduction pathways emanating from engineered cell substrates remains unclear. To elucidate the role, polymers derived from the amino acid L-tyrosine were used as synthetic matrix substrates. Variations in their chemical properties were created by co-polymerizing hydrophobic L-tyrosine derivatives with uncharged hydrophilic poly(ethylene glycol) (PEG, Mw = 1,000 Da), and negatively charged desaminotyrosyl-tyrosine (DT). These substrates were characterized for their intrinsic ability to generate ROS, as well as their ability to elicit Saos-2 cell responses in terms of intracellular ROS production, actin remodeling, and apoptosis. PEG-containing substrates induced both exogenous and intracellular ROS production, whereas the charged substrates reduced production of both types, indicating a coupling of exogenous ROS generation and intracellular ROS production. Furthermore, PEG-mediated ROS induction caused nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase and an increase in caspase-3 activity, confirming a link with apoptosis. PEG-rich pro-oxidant substrates caused cytoskeletal actin remodeling through beta-actin cleavage by caspase-3 into fractins. The fractins co-localized to the mitochondria and reduced the mitochondrial membrane potential. The remnant cytosolic beta-actin was polymerized and condensed, events consistent with apoptotic cell shrinkage. The cytoskeletal remodeling was integral to the further augmentation of intracellular ROS production. Conversely, the anti-oxidant DT-containing charged substrates suppressed the entire cascade of apoptotic progression. We demonstrate that ROS activity serves an important role in "outside-in" signaling for cells grown on substrates: the ROS activity couples exogenous stress, driven by substrate composition, to changes in intracellular signaling. This signaling causes cell apoptosis, which is mediated by actin remodeling.

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Section: Discussionmentioning

confidence: 89%

Synthetic polymeric substrates as potent pro‐oxidant versus anti‐oxidant regulators of cytoskeletal remodeling and cell apoptosis

Sung¹,

Chandra²,

Treiser³

et al. 2008

Journal Cellular Physiology

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“…During oxidation of proteins, the microenvironment of a given residue may alter the redox potential and influence the oxidation of other amino acids. Negatively charged residues adjacent to tyrosine enhance tyrosine oxidation, and positively charged residues hinder this effect . The redox potential of the .…”

Section: Radical Reactions On Proteinsmentioning

confidence: 99%

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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“…The degradation of the residue 1-12 region can be attributed to the oxidation of His-1 and Tyr-10 that is adjacent to the negatively charged Asp-9 residue which may bind to the Cu 2+ ions. The degradation of histidine by the H 2 O 2 /Cu 2+ system and the binding of the carboxyl group to Cu 2+ ion that catalyzes oxidation of nearby tyrosine (in Glu-Tyr and Nacetyltyrosine) have been studied and reported previously (7,8). On the contrary, when glucagon was oxidized by simulated sunlight at pH 9, Fragment (residue 1-12) became less susceptible to oxidation than in metal-catalyzed degradation ( Figs.…”

Section: Chromatography Of Oxidized Glucagonmentioning

confidence: 81%

Metal-Catalyzed Oxidation and Photo-oxidation of Glucagon

Zhang

2015

AAPS PharmSciTech

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The oxidation of glucagon by the H2O2/Cu(2+) system and by simulated sunlight was studied using HPLC-MS methodologies. It was found that copper ion-catalyzed oxidation is much faster in the residue 1-12 region than in photo-oxidation, but it is slower than photo-oxidation in the residue 18-29 region. This difference is due to the unique feature of the primary sequence of glucagon. The residue 1-12 region contains His-1 and Asp-9 that can bind to Cu(2+) ions and catalyze the oxidation of His-1 and Tyr-10, while the residue 18-29 region lacks these charged residues near the liable Met-27 and Trp-25 and hence no catalysis by the neighboring groups occurs. Fragment (residue 13-17) was more stable than the other regions of the peptide toward photo-oxidation because it contains only one oxidizable residue, Tyr-13. These findings may help explain the mechanism of action of glucagon and provide some hints for the development of effective anti-diabetic drug molecules and stable glucagon formulations.

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The effect of neighboring amino acid residues and solution environment on the oxidative stability of tyrosine in small peptides

Cited by 17 publications

References 30 publications

Synthetic polymeric substrates as potent pro‐oxidant versus anti‐oxidant regulators of cytoskeletal remodeling and cell apoptosis

Synthetic polymeric substrates as potent pro‐oxidant versus anti‐oxidant regulators of cytoskeletal remodeling and cell apoptosis

The Chemistry of Protein Oxidation in Food

Metal-Catalyzed Oxidation and Photo-oxidation of Glucagon

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