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Temperature-Dependent Antibody Kinetics as a Tool in Antibody Lead Selection

  • Michael SchrämlEmail author
  • Leopold von Proff
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 901)

Abstract

Antibody–antigen interactions can principally be classified into three different temperature-dependent kinetic rate profiles. The affinity K D can persist, decrease, or increase in the temperature gradient. Today, the impact of temperature-dependent antibody kinetics is recognized, especially as part of the development of best in class monoclonal antibodies. Here, a robust surface plasmon resonance-based protocol is presented, which describes a sensitive temperature-dependent kinetic measurement and evaluation method.

Key words

Surface plasmon resonance SPR Kinetics ka kd KD Temperature Thermodynamics 

References

  1. 1.
    Leonard P, Hayes CJ, O’Kennedy R (2011) Rapid temperature-dependent antibody ranking using Biacore A100. Anal Biochem 409: 290–292PubMedCrossRefGoogle Scholar
  2. 2.
    Roos H, Karlsson R, Nilshans H et al (1998) Thermodynamic analysis of protein interactions with biosensor technology. J Mol Recognit 11: 204–210PubMedCrossRefGoogle Scholar
  3. 3.
    Young L, Jernigan RL, Covell DG (1994) A role for surface hydrophobicity in protein–protein recognition. Protein Sci 3:717–729PubMedCrossRefGoogle Scholar
  4. 4.
    Willcox BE, Gao GF, Wyer JR et al (1999) TCR binding to peptide-MHC stabilizes a flexible recognition interface. Immunity 10:357–365PubMedCrossRefGoogle Scholar
  5. 5.
    Gabdoulline RR, Wade RC (2001) Protein-protein association: investigation of factors influencing association rates by brownian dynamics simulations. J Mol Biol 306:1139–1155PubMedCrossRefGoogle Scholar
  6. 6.
    Wang Y, Shen BJ, Sebald W (1997) A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain. Proc Natl Acad Sci U S A 94:1657–1662PubMedCrossRefGoogle Scholar
  7. 7.
    Stites WE (1997) Proteinminus signProtein interactions: interface structure, binding thermodynamics, and mutational analysis. Chem Rev 97:1233–1250PubMedCrossRefGoogle Scholar
  8. 8.
    Selzer T, Schreiber G (1999) Predicting the rate enhancement of protein complex formation from the electrostatic energy of interaction. J Mol Biol 287:409–419PubMedCrossRefGoogle Scholar
  9. 9.
    Sinha N, Smith-Gill SJ (2002) Electrostatics in protein binding and function. Curr Protein Pept Sci 3:601–614PubMedCrossRefGoogle Scholar
  10. 10.
    Zeder-Lutz G, Zuber E, Witz J et al (1997) Thermodynamic analysis of antigen–antibody binding using biosensor measurements at different temperatures. Anal Biochem 246: 123–132PubMedCrossRefGoogle Scholar
  11. 11.
    Pasqualucci L, Guglielmino R, Houldsworth J et al (2004) Expression of the AID protein in normal and neoplastic B cells. Blood 104: 3318–3325PubMedCrossRefGoogle Scholar
  12. 12.
    Torres M, Fernandez-Fuentes N, Fiser A et al (2007) Exchanging murine and human immunoglobulin constant chains affects the kinetics and thermodynamics of antigen binding and chimeric antibody autoreactivity. PLoS One 2:e1310PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2012

Authors and Affiliations

  1. 1.Roche Diagnostics GmbHPenzbergGermany

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