Detection of low-molecular-weight analytes by surface plasmon resonance and receptor conformational changes

2002 ◽  
Author(s):  
Helen V. Hsieh ◽  
Jason E. Gestwicki ◽  
J. B. Pitner
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Conformational Changes ◽  
Plasmon Resonance ◽  
Low Molecular Weight

Miniaturized portable surface plasmon resonance immunosensor applicable for on-site detection of low-molecular-weight analytes

2006 ◽  
Vol 115 (1) ◽  
pp. 349-356 ◽  
Author(s):  
Sook Jin Kim ◽  
K. Vengatajalabathy Gobi ◽  
Ryohei Harada ◽  
D. Ravi Shankaran ◽  
Norio Miura
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Low Molecular Weight

Detection of low-molecular-weight domoic acid using surface plasmon resonance sensor

2005 ◽  
Vol 107 (1) ◽  
pp. 193-201 ◽  
Author(s):  
Qiuming Yu ◽  
Shengfu Chen ◽  
Allen D. Taylor ◽  
Jiří Homola ◽  
Bertold Hock ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Domoic Acid ◽  
Low Molecular Weight ◽  
Surface Plasmon Resonance Sensor ◽  
Resonance Sensor

Capture and Analysis of Low Molecular Weight Ligands by Surface Plasmon Resonance Combined with Mass Spectrometry

2001 ◽  
Vol 7 (4-5) ◽  
pp. 385-391 ◽  
Author(s):  
Carsten P. Sönksen ◽  
Peter Roepstorff ◽  
Per-Olof Markgren ◽  
U. Helena Danielson ◽  
Markku D. Hämäläinen ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Electrospray Ionization ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Ion Trap ◽  
Low Molecular Weight ◽  
Maldi Tof ◽  
Hiv 1

The combination of biomolecular interaction analysis (BIA)by surface plasmon resonance (SPR)and nano-electrospray ionization ion trap mass spectrometry (nanoESI-Ion Trap MS)as well as matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToF MS)is demonstrated for the binding of low molecular weight inhibitors (∼ 600 Da) to HIV-1 protease. Inhibitors were captured on sensor chips of a manual or an automated SPR biosensor, to which HIV-1 protease was immobilized. Compounds and buffer components that bound unspecifically to the sensor surface were removed and the inhibitors were eluted in a minimal volume (3 μL), between air bubbles, in order to prevent dispersion of analyte into buffer eluent. Molecular weights were subsequently determined by mass spectrometry, structural information was obtained by MALDI-ToF post-source decay as well as by electrospray ionization tandem mass spectrometry (MS/MS)analysis. Furthermore, competition experiments, using a mixture of different ligands, demonstrated that the peak intensities in the MALDI-ToF spectrum could be used for relative quantification of the amount of the different ligands bound to the immobilized target. Methodology for automated capture and elution of analytes was developed and evaluated.

Colloidal Au Replacement Assay for Highly Sensitive Quantification of Low Molecular Weight Analytes by Surface Plasmon Resonance

2007 ◽  
Vol 18 (4) ◽  
pp. 1241-1245 ◽  
Author(s):  
Seiji Takae ◽  
Yoshitsugu Akiyama ◽  
Yuichi Yamasaki ◽  
Yukio Nagasaki ◽  
Kazunori Kataoka
Keyword(s):  
Molecular Weight ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Low Molecular Weight ◽  
Highly Sensitive ◽  
Colloidal Au
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