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
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
Journal title :
Applied Surface Science