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Chloramine T-induced structural and biochemical changes in echistatin

C C Kumar¹, H Nie, L Armstrong

¹Department of Tumor Biology, Schering-Plough Research Institute, Kenilworth, NJ 07033, USA. Chandra.kumar@spcorp.com

|July 14, 1998

Summary

Lactoperoxidase labeling preserves echistatin

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Area of Science:

Biochemistry
Molecular Biology
Integrin Biology

Background:

Echistatin is a disintegrin peptide inhibiting platelet aggregation and cell adhesion.
It binds integrin receptors alpha(v)beta3 and alpha(IIb)beta3 via an RGD motif.
Disulfide bonds maintain the RGD loop conformation crucial for binding.

Purpose of the Study:

To compare the binding characteristics of echistatin labeled by lactoperoxidase versus chloramine T methods.
To elucidate the structural impact of labeling on echistatin's receptor interaction.

Main Methods:

Iodination of echistatin using lactoperoxidase and chloramine T methods.
Assessment of echistatin binding affinity and dissociation kinetics to integrin alpha(v)beta3.
Molecular modeling and dynamic simulations to analyze structural changes.

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Main Results:

Lactoperoxidase-labeled echistatin exhibited high-affinity, non-dissociable binding to alpha(v)beta3, similar to native echistatin.
Chloramine T-labeled echistatin showed rapid dissociation from the receptor.
Chloramine T labeling resulted in oxidation of a methionine residue adjacent to the RGD motif.
Molecular simulations indicated hydrogen bonding between the oxidized methionine and the RGD motif.

Conclusions:

Lactoperoxidase labeling is a suitable method for maintaining echistatin's native binding properties.
Chloramine T labeling alters echistatin structure, leading to reduced receptor affinity and increased dissociation.
Oxidation of methionine by chloramine T directly impacts echistatin-integrin interactions.