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Issue 4, 2008
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OH radical reactions with phenylalanine in free and peptide forms

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Abstract

Density functional theory has been used to model the reaction of OH with L-phenylalanine, as a free molecule and in the Gly-Phe-Gly peptide. The influence of the environment has been investigated using water and benzene as models for polar and non-polar surroundings, in addition to gas phase calculations. Different paths of reaction have been considered, involving H abstractions and addition reactions, with global contributions to the overall reaction around 10% and 90% respectively when Phe is in its free form. The ortho-adducts (o-tyrosine) were found to be the major products of the Phe + OH reaction, for all the modeled environments and especially in water solutions. The reactivity of phenylalanine towards OH radical attacks is predicted to be higher in its peptidic form, compared to the free molecule. The peptidic environment also changes the sites’ reactivity, and for the Gly-Phe-Gly + OH reaction H abstraction becomes the major path of reaction. The good agreement found between the calculated and the available experimental data supports the methodology used in this work, as well as the data reported here for the first time.

Graphical abstract: OH radical reactions with phenylalanine in free and peptide forms

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Supplementary files

Article information


Submitted
18 Oct 2007
Accepted
14 Dec 2007
First published
11 Jan 2008

Org. Biomol. Chem., 2008,6, 732-738
Article type
Paper

OH radical reactions with phenylalanine in free and peptide forms

A. Galano and A. Cruz-Torres, Org. Biomol. Chem., 2008, 6, 732
DOI: 10.1039/B716024K

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