Abstract
(s)‐allantoin is one of the breakdown products of uric acid in many animals, including humans. It has been shown to be a product of the oxidation of uric acid. Allantoin concentration in plasma and urine has been correlated with the level of oxidative stress in the organism. The goal of this research is to study the binding modes of allantoin to natural binding partners for which allantoin is a product or substrate, and other unrelated proteins that bind with reasonable affinity. The proteins are first subjected to docking using Swiss‐Dock to identify binding clusters with optimized affinity. The most favorable are then subjected to ab initio quantum mechanical calculations on limited volumes around the binding sites using Gaussian. H‐bond networks and other interactions are predicted. The overall results have been used to design synthetic peptides with good predicted binding affinities. Besides adding to the understanding of allantoin binding to proteins, this method has applicability in designing detection methods for the presence of allantoin and related compounds.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
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