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Issue 4, 2001
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Intracellular oxidation of dipeptides. Very fast halogenation of the amino-terminal residue

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Abstract

Peptides undergo a very fast halogenation reaction with aqueous halogens. The process takes place via aliphatic electrophilic substitution with bimolecular rate constants of ca. 107 M−1 s−1. The products formed are N-halo-peptides, i.e., the halogenation process takes place on the nitrogen atom at the amino-terminal moiety of the amino acid residue. At ratios [halogenating agent]/[dipeptide] ≤ 1, no analytical or kinetic evidence has been found of halogenation on the peptide bond or on the oxygen atom of the carboxy-terminal residue. The intracellular oxidation of peptides to N-halo-peptides proceeds by an in vivo mechanism to reduce the oxidative stress caused by intracellular oxidants.

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Graphical abstract: Intracellular oxidation of dipeptides. Very fast halogenation of the amino-terminal residue

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Publication details

The article was received on 06 Sep 2000, accepted on 31 Jan 2001 and first published on 02 Mar 2001


Article type: Paper
DOI: 10.1039/B007208G
J. Chem. Soc., Perkin Trans. 2, 2001, 608-612

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    Intracellular oxidation of dipeptides. Very fast halogenation of the amino-terminal residue

    X. L. Armesto, M. Canle L., M. I. Fernández, M. V. García, S. Rodríguez and J. A. Santaballa, J. Chem. Soc., Perkin Trans. 2, 2001, 608
    DOI: 10.1039/B007208G

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