Grafting Hyaluronic Acid onto Gold Surface to Achieve Low Protein Fouling in Surface Plasmon Resonance Biosensors

2014 ◽  
Vol 6 (15) ◽  
pp. 13034-13042 ◽  
Author(s):  
Xia Liu ◽  
Renliang Huang ◽  
Rongxin Su ◽  
Wei Qi ◽  
Libing Wang ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Gold Surface ◽  
Low Protein ◽  
Protein Fouling

Localized and Propagating Surface Plasmon Resonance Sensors: A Study Using Carbohydrate Binding Protein

2005 ◽  
Vol 876 ◽  
Author(s):  
Chanda Yonzon ◽  
Richard P. Van Duyne
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Specific Binding ◽  
Gold Surface ◽  
Optical Biosensor ◽  
Localized Surface Plasmon ◽  
Carbohydrate Binding ◽  
Binding Studies ◽  
Assembled Monolayers

AbstractThis work encompasses a comparative analysis of the properties of two optical biosensor platforms: (1) the propagating surface plasmon resonance (SPR) sensor based on a planar, thin film gold surface and (2) the localized surface plasmon resonance (LSPR) sensor based on surface confined Ag nanoparticles fabricated by nanosphere lithography. The binding of Concanavalin A (ConA) to mannose-functionalized self-assembled monolayers (SAMs) is chosen to illustrate the similarities and the differences of these sensors. A comprehensive set of non-specific binding studies demonstrate that the single transduction mechanism is due to the specific binding of ConA to the mannose-functionalized surface. Finally, an elementary (2x1) multiplexed version of a LSPR carbohydrate sensing chip to probe the simultaneous binding of ConA to mannose and galactose-functionalized SAMs is also demonstrated.

scholarly journals A Surface Plasmon Resonance Biosensor Based on Directly Immobilized Hemoglobin and Myoglobin

Sensors ◽  
2020 ◽  
Vol 20 (19) ◽  
pp. 5572
Author(s):  
Georgi Dyankov ◽  
Ekaterina Borisova ◽  
Evdokia Belina ◽  
Hristo Kisov ◽  
Ivan Angelov ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Structural Integrity ◽  
Complex Structure ◽  
Gold Surface ◽  
Laser Evaporation ◽  
The Matrix ◽  
Direct Immobilization ◽  
The Impact

Immobilization of proteins on a surface plasmon resonance (SPR) transducer is a delicate procedure since loss of protein bioactivity can occur upon contact with the untreated metal surface. Solution to the problem is the use of an immobilization matrix having a complex structure. However, this is at the expense of biosensor selectivity and sensitivity. It has been shown that the matrix-assisted pulsed laser evaporation (MAPLE) method has been successfully applied for direct immobilization (without a built-in matrix) of proteins, preserving their bioactivity. So far, MAPLE deposition has not been performed on a gold surface as required for SPR biosensors. In this paper we study the impact of direct immobilization of heme proteins (hemoglobin (Hb) and myoglobin (Mb)) on their bioactivity. For the purpose, Hb and Mb were directly immobilized by MAPLE technique on a SPR transducer. The bioactivity of the ligands immobilized in the above-mentioned way was assessed by SPR registration of the molecular reactions of various Hb/Mb functional groups. By SPR we studied the reaction between the beta chain of the Hb molecule and glucose, which shows the structural integrity of the immobilized Hb. A supplementary study of films deposited by FTIR and AFM was provided. The experimental facts showed that direct immobilization of an intact molecule was achieved.

Investigation of amorphous SiOx layer on gold surface for Surface Plasmon Resonance measurements

2016 ◽  
Vol 163 ◽  
pp. 43-48 ◽  
Author(s):  
Etienne Herth ◽  
Rabah Zeggari ◽  
Jean-Yves Rauch ◽  
Fabien Remy-Martin ◽  
Wilfrid Boireau
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Gold Surface
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