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Updated: May 9, 2026
Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Specificity and regenerability of short peptide ligands supported on polymer layers for immunoglobulin G binding and
Yanxia Zhang1, Nafisa Islam, Ruben G Carbonell
1Department of Forest Biomaterials, North Carolina State University, Raleigh, North Carolina 27695, USA. yzhang58@ncsu.edu
We demonstrate the specificity, regenerability, and excellent storage stability of short peptide-based systems for detection of immunoglobulin G (IgG). The bioactive component consisted of acetylated-HWRGWVA (Ac-HWRGWVA), a peptide with high IgG binding affinity, which was immobilized onto copolymer matrixes of poly(2-aminoethyl methacrylate hydrochloride-co-2-hydroxyethyl methacrylate) (poly(AMA-co-HEMA)). Surface plasmon resonance (SPR) and quartz crystal microgravimetry (QCM) were utilized with other complementary techniques to systematically investigate interfacial activities, mainly IgG binding performance as a function of the graft density and degree of polymerization of the poly(AMA-co-HEMA) support layer. Results from sodium dodecyl sulfate polyacrylamide gel electrophoresis and fluorescence microscopy indicate that the bioactive system is highly specific to IgG and resistant to nonspecific interactions when tested in mixed protein solutions.
We demonstrate the specificity, regenerability, and excellent storage stability of short peptide-based systems for detection of immunoglobulin G (IgG). The bioactive component consisted of acetylated-HWRGWVA (Ac-HWRGWVA), a peptide with high IgG binding affinity, which was immobilized onto copolymer matrixes of poly(2-aminoethyl methacrylate hydrochloride-co-2-hydroxyethyl methacrylate) (poly(AMA-co-HEMA)). Surface plasmon resonance (SPR) and quartz crystal microgravimetry (QCM) were utilized with other complementary techniques to systematically investigate interfacial activities, mainly IgG binding performance as a function of the graft density and degree of polymerization of the poly(AMA-co-HEMA) support layer. Results from sodium dodecyl sulfate polyacrylamide gel electrophoresis and fluorescence microscopy indicate that the bioactive system is highly specific to IgG and resistant to nonspecific interactions when tested in mixed protein solutions.
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