Preparation of N-acetyl, tert-butyl amide derivatives of the 20 natural amino acids

Ekkati, Anil R.; Campanali, Ashley A.; Abouelatta, Ahmed I.; Shamoun, Mark; Kalapugama, Suneth; Kelley, Michael S. P.; Kodanko, Jeremy J.

doi:10.1007/s00726-009-0279-y

Cited by 5 publications

(3 citation statements)

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“…The complex [Fe II (N4Py)(CH 3 CN)](ClO 4 ) 2 , used in this study, was synthesized according to a literature procedure . The syntheses of substrates for these studies, of the general formula Ac-AA-NHtBu, where AA = amino acid, are described elsewhere . An experimental procedure and characterization data for the oxidation products of Ac-Gly-NHtBu obtained under catalytic conditions were described previously .…”

Section: Methodsmentioning

confidence: 99%

“…75 The syntheses of substrates for these studies, of the general formula Ac-AA-NHtBu, where AA = amino acid, are described elsewhere. 76 An experimental procedure and characterization data for the oxidation products of Ac-Gly-NHtBu obtained under catalytic conditions were described previously. 59 Reactions were performed under ambient atmosphere unless otherwise noted.…”

Section: Methodsmentioning

confidence: 99%

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Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

et al. 2009

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Kinetic and mechanistic studies detailing the oxidation of substrates derived from the 20 natural amino acids by the ferryl complex [Fe(IV)(O)(N4Py)](2+) are described. Substrates of the general formula Ac-AA-NHtBu were treated with the ferryl complex under identical conditions ([Ac-AA-NHtBu] = 10 mM, [Fe] = 1 mM, 1:1 H(2)O/CH(3)CN), and pseudo-first-order rate constants were obtained. Relative rate constants calculated from these data illustrated the five most reactive substrates; in order of decreasing reactivity were those derived from Cys, Tyr, Trp, Met, and Gly. Second-order rate constants were determined for these substrates by varying substrate concentration under pseudo-first-order conditions. Substrates derived from the other natural amino acids did not display significant reactivity, accelerating decomposition of the ferryl complex at a rate less than 10 times that of the control reaction with no substrate added. Ferryl decomposition rates changed in D(2)O/CD(3)CN for the Cys, Tyr, and Trp substrates, giving deuterium kinetic isotope effects of 4.3, 29, and 5.2, respectively, consistent with electron-transfer, proton-transfer (Cys and Trp), or hydrogen atom abstraction (Tyr) mechanisms. Decomposition rates for [Fe(IV)(O)(N4Py)](2+) in the presence of the Met and Gly substrates were identical in H(2)O/CH(3)CN versus D(2)O/CD(3)CN solvents. A deuterium kinetic isotope effect of 4.8 was observed with the labeled substrate 2,2-d(2)-Ac-Gly-NHtBu, consistent with [Fe(IV)(O)(N4Py)](2+) abstracting an alpha-hydrogen atom from Ac-Gly-NHtBu and generating a glycyl radical. Abstraction of alpha-hydrogen atoms from amino acid substrates other than Gly and oxidation of side chains contained in the amino acids other than Cys, Tyr, Trp, and Met were slow by comparison.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

et al. 2009

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“…General Procedure for the Synthesis of N-Acetylated Amino Acid t-Butyl Amides. 75 The N-acetylated amino acid (42.4 mmol) and p-nitrophenol (5.89 g, 42.4 mmol) were dissolved in dichloromethane (75 mL). N,N′-Dicyclohexyl carbodiimide (DCC, 8.79 g, 42.6 mmol) was added in portions.…”

Section: The Journal Of Organic Chemistrymentioning

confidence: 99%

Oxidative Damage in Aliphatic Amino Acids and Di- and Tripeptides by the Environmental Free Radical Oxidant NO₃^•: The Role of the Amide Bond Revealed by Kinetic and Computational Studies

Nathanael

Wille

2019

J. Org. Chem.

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Kinetic and computational data reveal a complex behavior of the important environmental free radical oxidant NO3 • in its reactions with aliphatic amino acids and di- and tripeptides, suggesting that attack at the amide N–H bond in the peptide backbone is a highly viable pathway, which proceeds through a proton-coupled electron transfer (PCET) mechanism with a rate coefficient of about 1 × 106 M–1 s–1 in acetonitrile. Similar rate coefficients were determined for hydrogen abstraction from the α-carbon and from tertiary C–H bonds in the side chain. The obtained rate coefficients for the reaction of NO3 • with aliphatic di- and tripeptides suggest that attack occurs at all of these sites in each individual amino acid residue, which makes aliphatic peptide sequences highly vulnerable to NO3 •-induced oxidative damage. No evidence for amide neighboring group effects, which have previously been found to facilitate radical-induced side-chain damage in phenylalanine, was found for the reaction of NO3 • with side chains in aliphatic peptides.

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High‐Valent Cr, Mn, and Fe Species

2012

Oxidation of Amino Acids, Peptides, and Proteins

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Preparation of N-acetyl, tert-butyl amide derivatives of the 20 natural amino acids

Cited by 5 publications

References 13 publications

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

Oxidative Damage in Aliphatic Amino Acids and Di- and Tripeptides by the Environmental Free Radical Oxidant NO₃^•: The Role of the Amide Bond Revealed by Kinetic and Computational Studies

High‐Valent Cr, Mn, and Fe Species

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Preparation of N-acetyl, tert-butyl amide derivatives of the 20 natural amino acids

Cited by 5 publications

References 13 publications

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

Oxidation of the Natural Amino Acids by a Ferryl Complex: Kinetic and Mechanistic Studies with Peptide Model Compounds

Oxidative Damage in Aliphatic Amino Acids and Di- and Tripeptides by the Environmental Free Radical Oxidant NO3•: The Role of the Amide Bond Revealed by Kinetic and Computational Studies

High‐Valent Cr, Mn, and Fe Species

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Product

Resources

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Oxidative Damage in Aliphatic Amino Acids and Di- and Tripeptides by the Environmental Free Radical Oxidant NO₃^•: The Role of the Amide Bond Revealed by Kinetic and Computational Studies