@article{yang_gurgel_williams_bobay_cavanagh_muddiman_carbonell_2010, title={Binding site on human immunoglobulin G for the affinity ligand HWRGWV}, volume={23}, number={3}, journal={Journal of Molecular Recognition}, author={Yang, H. O. and Gurgel, P. V. and Williams, D. K. and Bobay, B. G. and Cavanagh, J. and Muddiman, D. C. and Carbonell, R. G.}, year={2010}, pages={271–282} }
 @article{yang_gurgel_carbonell_2009, title={Purification of human immunoglobulin G via Fc-specific small peptide ligand affinity chromatography}, volume={1216}, ISSN={["1873-3778"]}, DOI={10.1016/j.chroma.2008.12.004}, abstractNote={Chromatographic resins of a family of linear Fc-binding hexamer peptides (HWRGWV, HYFKFD, and HFRRHL) exhibited the ability to selectively adsorb and isolate human IgG (hIgG) from complete mammalian cell culture medium (cMEM). Among them, the HWRGWV resin with a peptide density of 0.08 mequiv./g of resin was able to purify hIgG from cMEM with both purity and yield as high as 95%, comparable to Protein A and A2P agarose gels. The influences of N-terminal acetylation of the HWRGWV resin, ligand density on the resin, initial hIgG concentration, and temperature on IgG isolation were also investigated. The results indicate that these small peptide ligands, especially HWRGWV, offer a potential alternative to the use of Protein A or Protein G for large scale affinity chromatography.}, number={6}, journal={JOURNAL OF CHROMATOGRAPHY A}, author={Yang, Haiou and Gurgel, Patrick V. and Carbonell, Ruben G.}, year={2009}, month={Feb}, pages={910–918} }
 @article{yang_gurgel_carbonell_2005, title={Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G}, volume={66}, ISSN={["1397-002X"]}, DOI={10.1111/j.1747-0285.2006.00342.x}, abstractNote={Abstract:  A family of linear hexapeptides composed of histidine on the N‐terminus followed by aromatic amino acid(s) and positively charged amino acid(s) has been identified through a three‐step screening of a synthetic solid phase library. These peptides were able to recognize human immunoglobulin G (HIgG) through its Fc region, and their selectivity to Fc is comparable to Protein A. This is the first known report of short peptides that are able to bind HIgG by recognizing its Fc portion. One of the ligands from the identified family, HWRGWV, was examined for its ability to isolate HIgG from complex mixtures. It was found that HWRGWV possessed the potential to purify HIgG from complete mammalian cell culture medium containing 10% fetal calf serum with purity comparable to commercially available resins, but using milder elution conditions. HWRGWV bound all HIgG subclasses and IgGs from bovine, mouse, goat, and rabbit. The broad affinity spectrum as well as its Fc recognition ability may be useful in capturing and detecting both polyclonal and monoclonal antibodies.}, journal={JOURNAL OF PEPTIDE RESEARCH}, author={Yang, H and Gurgel, PV and Carbonell, RG}, year={2005}, month={Dec}, pages={120–137} }
 @misc{carbonell_yang_gurgel, title={Purification of immunoglobulins using affinity chromatography and peptide ligands}, volume={7,408,030}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Carbonell, R. G. and Yang, H. and Gurgel, P. V.} }