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Probing cocaine-antibody interactions in buffer and human serum.

Muthu Ramakrishnan | Fernando Alves De Melo | Berma M Kinsey | John E Ladbury | Thomas R Kosten | Frank M Orson
PloS one | 2012

Despite progress in cocaine immunotherapy, the kinetic and thermodynamic properties of antibodies which bind to cocaine and its metabolites are not well understood. It is also not clear how the interactions between them differ in a complex matrix such as the serum present in the human body. In the present study, we have used microscale thermophoresis (MST), isothermal titration calorimetry (ITC), and surface plasmon resonance (SPR) we have evaluated the affinity properties of a representative mouse monoclonal (mAb08) as well as those of polyclonal antibodies purified from vaccinated mouse and human patient serum.

Pubmed ID: 22859949

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Associated grants

  • Agency: NIDA NIH HHS, United States
    Id: 1X02DA032939
  • Agency: NIDA NIH HHS, United States
    Id: 5R01DA030338
  • Agency: NIDA NIH HHS, United States
    Id: DP1 DA033502
  • Agency: NIDA NIH HHS, United States
    Id: P50-DA18197
  • Agency: NIDA NIH HHS, United States
    Id: R01 DA023979
  • Agency: NIDA NIH HHS, United States
    Id: R01 DA026859
  • Agency: NIDA NIH HHS, United States
    Id: K05 DA 0454
  • Agency: NIDA NIH HHS, United States
    Id: P50 DA018197
  • Agency: NIDA NIH HHS, United States
    Id: 3R01DA023979
  • Agency: NIDA NIH HHS, United States
    Id: R01 DA030338
  • Agency: NIDA NIH HHS, United States
    Id: K05 DA000454
  • Agency: NIDA NIH HHS, United States
    Id: R01DA026859

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