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Affinity interactions of human immunoglobulin G with short peptides: role of ligand spacer on binding, kinetics, and mass transfer

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Abstract

The interaction affinity between human IgG and a short peptide ligand (hexameric HWRGWV) was investigated by following the shifts in frequency and energy dissipation in a quartz crystal microbalance (QCM). HWRGWV was immobilized by means of poly(ethylene glycol) tethered on QCM sensors coated with silicon oxide, which enhanced the accessibility of the peptide to hIgG and also passivated the surface. Ellipsometry and ToF-SIMS were employed for surface characterization. The peptide ligand density was optimized to 0.88 chains nm−2, which enabled the interaction of each hIgG molecule with at least one ligand. The maximum binding capacity was found to be 4.6 mg m−2, corresponding to a monolayer of hIgG, similar to the values for chromatographic resins. Dissociation constants were lower than those obtained from resins, possibly due to overestimation of bound mass by QCM. Equilibrium thermodynamic and kinetic parameters were determined, shedding light on interfacial effects important for detection and bioseparation.

The interaction affinity between human IgG and a short peptide ligand was investigated by using quartz crystal microgravimetry, ellipsometry and ToF-SIMS. Equilibrium thermodynamic and kinetics parameters were determined, shedding light on interfacial effects important for detection and bioseparation.

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Acknowledgments

The authors acknowledge the financial support from Pathogen Removal and Diagnostic Technologies (PRDT), a subsidiary of ProMetic BioSciences Inc. O.J.R. is grateful for funding support by the Academy of Finland through its Center of Excellence Program (2014–2019) “Molecular Engineering of Biosynthetic Hybrid Materials Research” (HYBER).

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Author notes

  1. Fei Shen

    Present address: Illumina Inc., 5200 Illumina Way, San Diego, CA, 92122, USA

Authors and Affiliations

  1. Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC, 27695-7095, USA

    Fei Shen, Orlando J. Rojas, Jan Genzer, Patrick V. Gurgel & Ruben G. Carbonell

  2. Department of Forest Biomaterials, North Carolina State University, Raleigh, NC, 27695-8005, USA

    Orlando J. Rojas

  3. Biobased Colloids and Materials (BiCMat), School of Chemical Technology, Aalto University, P. O. Box 16300, 00076, Aalto, Finland

    Orlando J. Rojas

  4. ProMetic BioSciences USA, Raleigh, NC, 27695, USA

    Patrick V. Gurgel

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  1. Fei Shen
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Correspondence to Orlando J. Rojas.

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Additional information

Published in the topical collection Analytical Applications of Biomimetic Recognition Elements with guest editors Maria C. Moreno-Bondi and Elena Benito-Peña.

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Shen, F., Rojas, O.J., Genzer, J. et al. Affinity interactions of human immunoglobulin G with short peptides: role of ligand spacer on binding, kinetics, and mass transfer. Anal Bioanal Chem 408, 1829–1841 (2016). https://doi.org/10.1007/s00216-015-9135-y

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  • DOI: https://doi.org/10.1007/s00216-015-9135-y

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