@article{wang_carbonell_2006, title={Design of adsorptive columns for specific pathogen removal: Application to staphylococcal enterotoxin B}, volume={22}, DOI={10.1021/pb060126l}, number={5}, journal={Biotechnology Progress}, author={Wang, G. Q. and Carbonell, R. G.}, year={2006}, pages={1358–1367} }
 @article{wang_carbonell_2005, title={Characterization of a peptide affinity support that binds selectively to staphylococcal enterotoxin B}, volume={1078}, ISSN={["1873-3778"]}, DOI={10.1016/j.chroma.2005.05.010}, abstractNote={The influences of mass transfer and adsorption-desorption kinetics on the binding of staphylococcal enterotoxin B (SEB) to an affinity resin with the peptide ligand, Tyr-Tyr-Trp-Leu-His-His (YYWLHH) have been studied. The bed and particle porosities, the axial dispersion coefficient and the pore diffusivity were measured using pulse experiments under unretained conditions. Adsorption isotherms for SEB on YYWLHH resins with peptide densities in the range from 6 to 220 micromol/g were measured and fitted to a bi-Langmuir equation. At peptide densities below 9 micromol/g and above 50 micromol/g, dissociation constants were lower (2 x 10(-3) to 7 x 10(-3) mol/m3), and binding capacities were larger (43-47 mg SEB/g). In the range from 9 to 50 micromol/g dissociation constants were larger (13 x 10(-3) to 24 x 10(-3) mol/m3) and capacities were lower (33-37 mg SEB/g). These observations are consistent with a transition from single point attachment of the protein to the ligand at low peptide densities to multipoint attachment at high peptide densities. The general rate (GR) model of chromatography was used to fit experimental breakthrough curves under retained conditions to determine the intrinsic rate constants for adsorption, which varied from 0.13 to 0.50 m3 mol(-1) s(-1), and exhibited no clear trend with increasing peptide density. An analysis of the number of transfer units for the various mass transfer steps in the column indicated that film mass transfer, pore diffusion (POR) and the kinetics of adsorption can all play an important role in the overall rate of adsorption, with the intrinsic adsorption step apparently being the rate determining step at peptide densities below 50 micromol/g.}, number={1-2}, journal={JOURNAL OF CHROMATOGRAPHY A}, author={Wang, GQ and Carbonell, RG}, year={2005}, month={Jun}, pages={98–112} }
 @article{wang_de_schoeniger_roe_carbonell_2004, title={A hexamer peptide ligand that binds selectively to staphylococcal enterotoxin B: isolation from a solid phase combinatorial library}, volume={64}, ISSN={["1397-002X"]}, DOI={10.1111/j.1399-3011.2004.00170.x}, abstractNote={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.}, number={2}, journal={JOURNAL OF PEPTIDE RESEARCH}, author={Wang, G and De, J and Schoeniger, JS and Roe, DC and Carbonell, RG}, year={2004}, month={Aug}, pages={51–64} }