Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Authors

  • H. Yang,

    1. H. Yang, P.V. Gurgel and R.G. Carbonell, Department of Chemical and Biomolecular Engineering, North Carolina State University, Partners I, Suite 3500, Box 7565, Raleigh, NC 27695-7565, USA
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  • P.V. Gurgel,

    1. H. Yang, P.V. Gurgel and R.G. Carbonell, Department of Chemical and Biomolecular Engineering, North Carolina State University, Partners I, Suite 3500, Box 7565, Raleigh, NC 27695-7565, USA
    Search for more papers by this author
  • R.G. Carbonell

    1. H. Yang, P.V. Gurgel and R.G. Carbonell, Department of Chemical and Biomolecular Engineering, North Carolina State University, Partners I, Suite 3500, Box 7565, Raleigh, NC 27695-7565, USA
    Search for more papers by this author

R.G. Carbonell
Department of Chemical and Biomolecular Engineering
North Carolina State University
Partners I
Suite 3500
Box 7565
Raleigh
NC 27695-7565
USA
Tel.: 1-919-515-5118
Fax: 1-919-515-5831
E-mail: ruben@ncsu.edu

Abstract

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.

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