Thermodynamic and structural analysis of interactions between peptide ligands and SEB


Dudak F. C. , Soykut E. A. , Oguz M. E. , YAŞAR F. , BOYACI İ. H.

JOURNAL OF MOLECULAR RECOGNITION, cilt.23, sa.4, ss.369-378, 2010 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 23 Konu: 4
  • Basım Tarihi: 2010
  • Doi Numarası: 10.1002/jmr.1003
  • Dergi Adı: JOURNAL OF MOLECULAR RECOGNITION
  • Sayfa Sayıları: ss.369-378

Özet

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 (C) 2009 John Wiley & Sons, Ltd.