2007
DOI: 10.1208/pt0804102
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The effect of neighboring amino acid residues and solution environment on the oxidative stability of tyrosine in small peptides

Abstract: The effects of neighboring residues and formulation variables on tyrosine oxidation were investigated in model dipeptides (glysyl tyrosine, N-acetyl tyrosine, glutamyl tyrosine, and tyrosyl arginine) and tripeptide (lysyl tyrosyl lysine). The tyrosyl peptides were oxidized by light under alkaline conditions by a zero-order reaction. The rate of the photoreaction was dependent on tyrosyl pK a , which was perturbed by the presence of neighboring charged amino acid residues. The strength of light exposure, oxygen… Show more

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Cited by 17 publications
(10 citation statements)
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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%
“…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%
“…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 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%