Inhibition of Lysozyme by Taurine Dibromamine

Author(s): M. S. Petronio, V. F. Ximenes

Journal Name: Protein & Peptide Letters

Volume 20 , Issue 11 , 2013

Become EABM
Become Reviewer
Call for Editor


Hypobromous acid (HOBr) is a powerful oxidant produced by stimulated neutrophils and eosinophils. Taurine, a non-protein amino acid present in high amounts in the leukocytes, reacts instantaneously with HOBr leading to their haloamine derivative taurine dibromamine (Tau-NBr2). Lysozyme is a bactericidal enzyme also present in leukocytes and in secretory fluids. The inhibition of lysozyme is a pathway for bacterial proliferation in inflammatory sites. Here, we investigated the inhibition of the enzymatic activity of lysozyme when it was submitted to oxidation by Tau-NBr2. We found that the oxidation of lysozyme by Tau-NBr2 decreased its enzymatic activity in 80%, which was significant higher compared to the effect of its precursor HOBr (30%). The study and comparison of Tau-NBr2 and HOBr regarding the alterations provoked in the intrinsic fluorescence, synchronous fluorescence, resonance light scattering and near and far-UV circular dichroism spectra of lysozyme and oxidized lysozyme revealed that tryptophan residues in the active site of the protein were the main target for Tau-NBr2 and could explain its efficacy as inhibitor of lysozyme enzymatic activity. This property of Tau-NBr2 may have pathological significance, since it can be easily produced in the inflammatory sites.

Keywords: Eosinophils, hypobromous acid, hypochlorous acid, lysozyme, neutrophils, taurine dibromamine.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2013
Published on: 13 September, 2013
Page: [1232 - 1237]
Pages: 6
DOI: 10.2174/0929866511320110007
Price: $65

Article Metrics

PDF: 11