A direct human heart-type fatty acid binding protein (HFABP) immunosensor was
developed using anti- HFABP monoclonal antibodies (MAbs) immobilized on the gold
surface of a self-assembled surface plasmon resonance (SPR) apparatus. A kind of
self-assembled monolayer (SAM) prepared by cystamine-protein Amethod was applied
to immobilize the MAbs. Ten cycles of measurements could be performed on the same
chip regenerated with a 0.1 M HCl solution. A linear relationship existed between the
angle shifts (millidegrees) and the log values of HFABP concentrations in the range
from 0.1 to 300 ng/mL in buffer and artificial human serum. When used for 15 days,
the angle shifts were all >95% of those on the response at the first day. A 1 M NaOH
solution was used for clearing nonspecific binding in artifical human serum. The SPR
sensor offers advantages of simplicity of immobilization, high sensitivity, high
specificity, low sample requirement, high reusability, no label and no pretreatment etc.
