Comparison of HNO reactivity with tryptophan and cysteine in small peptides

Gizem Keceli; Cathy D Moore; John P Toscano

doi:10.1016/j.bmcl.2014.07.014

Comparison of HNO reactivity with tryptophan and cysteine in small peptides

Bioorg Med Chem Lett. 2014 Aug 15;24(16):3710-3. doi: 10.1016/j.bmcl.2014.07.014. Epub 2014 Jul 12.

Authors

Gizem Keceli¹, Cathy D Moore¹, John P Toscano²

Affiliations

¹ Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, United States.
² Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218, United States. Electronic address: jtoscano@jhu.edu.

PMID: 25080164
DOI: 10.1016/j.bmcl.2014.07.014

Abstract

Recent discoveries of important pharmacological properties have drawn attention to the reactivity of HNO (azanone, nitroxyl) with biologically relevant substrates. Apart from its role in thiol oxidation, HNO has been reported to have nitrosative properties, for example, with tryptophan resulting in N-nitrosotryptophan formation. We have investigated the reactivity of HNO with tryptophan and small peptides containing either tryptophan or both a tryptophan and a cysteine residue. Our results point to the more reactive nature of cysteine towards HNO compared with tryptophan.

Keywords: Cysteine- and tryptophan-containing peptides; HNO; HNO-derived N-nitrosotryptophan.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Cysteine / chemistry*
Molecular Structure
Nitrogen Oxides / chemistry*
Peptides / chemistry*
Tryptophan / chemistry*

Substances

Nitrogen Oxides
Peptides
Tryptophan
nitroxyl
Cysteine