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Thermodynamic and structural analysis of interactions between peptide ligands and SEB

✍ Scribed by Fahriye Ceyda Dudak; Esra Acar Soykut; Murat Erman Oğuz; Fatih Yaşar; İsmail Hakkı Boyacı

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
573 KB
Volume
23
Category
Article
ISSN
0952-3499

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✦ Synopsis

Abstract

Staphylococcal enterotoxin B (SEB) is an exotoxin produced by Staphylococcus aureus and commonly associated with food poisoning. In this study, SEB‐binding peptides were identified by screening a phage displayed peptide library. The binding of peptides to SEB was tested with isothermal titration calorimetry (ITC) and of the five selected peptides, three showed affinity to SEB, with one measured to have the highest affinity constant (10^5^ M^−1^). ITC revealed that the interaction of peptide ligands with SEB was driven entropically and the binding was dominated by hydrophobic interactions. Circular dichroism (CD) measurements and molecular dynamics (MD) simulations, together, give a structural insight into the interaction of peptides with SEB. While SEB binding peptides showed random coil structure before binding, after complex formation they had more ordered structures. The peptide with highest affinity to SEB showed stable conformation during MD simulation. Taken together, our approach about thermodynamic and structural characterization of peptide ligands can be used to develop aptamers, with high affinity and selectivity, for biosensor applications. Copyright © 2009 John Wiley & Sons, Ltd.

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