A hexamer peptide ligand that binds selectively to staphylococcal enterotoxin B: isolation from a solid phase combinatorial library

The Journal of Peptide Research : Official Journal of the American Peptide Society
G WangR G Carbonell

Abstract

By screening a solid-phase combinatorial peptide library, a short peptide ligand, YYWLHH, has been discovered that binds with high affinity and selectivity to staphylococcal enterotoxin B (SEB), but only weakly to other SEs that share sequence and structural homology with SEB. Using column affinity chromatography with an immobilized YYWLHH stationary phase, it was possible to separate SEB quantitatively from Staphylococcus aureus fermentation broth, a complex mixture of proteins, carbohydrates and other biomolecules. The immobilized peptide was also used to purify native SEB from a mixture containing denatured and hydrolyzed SEB, and showed little cross-reactivity with other SEs. To our knowledge this is the first report of a highly specific short peptide ligand for SEB. Such a ligand is a potential candidate to replace antibodies for detection, removal and purification strategies for SEB.

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Citations

Jun 27, 2012·Biopolymers·Fahriye Ceyda DudakIsmail Hakkı Boyacı
Nov 27, 2009·Journal of Molecular Recognition : JMR·Fahriye Ceyda DudakIsmail Hakki Boyaci
Dec 18, 2007·Analytical Biochemistry·Heide DaxeckerNiamh Moran
Oct 26, 2005·Journal of Chromatography. a·Yannis D Clonis
Oct 7, 2006·Biotechnology Progress·Guangquan Wang, Ruben G Carbonell
Oct 17, 2014·Journal of Molecular Recognition : JMR·Joshua M KogotDimitra N Stratis-Cullum
Jun 22, 2005·Expert Review of Proteomics·Sun W TamDouglas Hinerfeld
Dec 15, 2007·Nature Protocols·Julia Tait Lathrop, David Hammond
Sep 5, 2013·Analytical Chemistry·Stefano MenegattiRuben Guillermo Carbonell

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