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Thermodynamic and structural analysis of interactions between peptide ligands and SEB
Author(s) -
Dudak Fahriye Ceyda,
Soykut Esra Acar,
Oğuz Murat Erman,
Yaşar Fatih,
Boyacı İsmail Hakkı
Publication year - 2010
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.1003
Subject(s) - isothermal titration calorimetry , chemistry , phage display , peptide , circular dichroism , random coil , binding constant , enterotoxin , peptide library , stereochemistry , combinatorial chemistry , binding site , crystallography , biochemistry , peptide sequence , escherichia coli , gene
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.