TY - JOUR
T1 - Using competitive protein adsorption to measure fibrinogen in undiluted human serum
AU - Choi, Seokheun
AU - Wang, Ran
AU - Lajevardi-Khosh, Arad
AU - Chae, Junseok
N1 - Funding Information:
The authors would like to thank Ms. Steele for valuable discussions. This work is partially supported by the NSF (Grant No. ECCS-#0846961).
PY - 2010/12/20
Y1 - 2010/12/20
N2 - We report a unique sensing mechanism based on competitive protein adsorption to measure fibrinogen, a cardiovascular biomarker, in undiluted human serum. The method uses physical adsorption of proteins to a surface rather than complex and time-consuming immobilization procedures. Two fibrinogen concentrations were differentiated in spiked in human serum [3.0 mg/ml (normal concentration) versus 3.2 mg/ml (abnormal concentration with heart disease)]. Real-time surface plasmon resonance signals were monitored as fibrinogen displaced a preadsorbed protein, IgM, on a hydrophobic gold surface. The relatively strong-affinity protein, IgM, was displaced primarily by fibrinogen and much less by other proteins in human serum.
AB - We report a unique sensing mechanism based on competitive protein adsorption to measure fibrinogen, a cardiovascular biomarker, in undiluted human serum. The method uses physical adsorption of proteins to a surface rather than complex and time-consuming immobilization procedures. Two fibrinogen concentrations were differentiated in spiked in human serum [3.0 mg/ml (normal concentration) versus 3.2 mg/ml (abnormal concentration with heart disease)]. Real-time surface plasmon resonance signals were monitored as fibrinogen displaced a preadsorbed protein, IgM, on a hydrophobic gold surface. The relatively strong-affinity protein, IgM, was displaced primarily by fibrinogen and much less by other proteins in human serum.
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U2 - 10.1063/1.3529445
DO - 10.1063/1.3529445
M3 - Article
AN - SCOPUS:78650740545
SN - 0003-6951
VL - 97
JO - Applied Physics Letters
JF - Applied Physics Letters
IS - 25
M1 - 253701
ER -