• Title of article

    ToF-SIMS surface and interface characterization of the immobilized camel antibody (cAb) onto SAMs-COOH/Au substrates

  • Author/Authors

    A. Azioune، نويسنده , , J.-J. Pireaux، نويسنده , , L. Houssiau، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2004
  • Pages
    4
  • From page
    402
  • To page
    405
  • Abstract
    Carboxyl terminated SAMs were deposited onto gold substrates to immobilize the highly stable camel antibody (cAb) which is responsible for prostate specific antigen (PSA) recognition. ToF-SIMS was used in the static mode to follow the surface chemistry at the different stages of surface treatment. First, the thiol (11-mercaptoundecanoic acid) adsorption on the gold substrates was clearly identified by means of the deprotonated molecular fragment (C11H21O2S ) at m/z ¼ 217. Then the activator of carboxylic groups (1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride, or EDC) was identified by several specific fragments (e.g. C3H8Nþ). Finally, the cAb immobilization at different initial solution concentrations was followed by ToF-SIMS, using the technique’s molecular sensitivity. We identified some amino acids fragments clearly increasing with the solution concentration (e.g. C7H7Oþ, C8H10NOþ). The cAb immobilization was also measured by the gradual disappearance of the coupling agent. This study is therefore an attempt to quantify the antibody immobilization by using carefully selected molecular ions, different from those emitted from the substrate and/or adventitious organic contaminants. # 2004 Elsevier B.V. All rights reserved.
  • Keywords
    Protein immobilization , Camel antibody , ToF-SIMS , amino acids , Biosensors , SAM
  • Journal title
    Applied Surface Science
  • Serial Year
    2004
  • Journal title
    Applied Surface Science
  • Record number

    999627