Specific Binding of Immunoglobulin G with Bioactive Short Peptides Supported on Antifouling Copolymer Layers for Detection in Quartz Crystal Microgravimetry and Surface Plasmon Resonance

2012 ◽  
Vol 85 (2) ◽  
pp. 1106-1113 ◽  
Author(s):  
Yanxia Zhang ◽  
Nafisa Islam ◽  
Ruben G. Carbonell ◽  
Orlando J. Rojas
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Immunoglobulin G ◽  
Quartz Crystal ◽  
Specific Binding ◽  
Short Peptides ◽  
Quartz Crystal Microgravimetry

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.

SURFACE PLASMON RESONANCE SPECTROSCOPY AND QUARTZ CRYSTAL MICROBALANCE STUDY OF PROTEIN-DNA INTERACTIONS IN HORMONE RECEPTOR BIOLOGY

COSMOS ◽  
2009 ◽  
Vol 05 (01) ◽  
pp. 79-95
Author(s):  
XIAODI SU
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Quartz Crystal Microbalance ◽  
Conformational Changes ◽  
Plasmon Resonance ◽  
Quartz Crystal ◽  
Resonance Spectroscopy ◽  
Dna Interactions ◽  
Protein Dna Interactions

Surface plasmon resonance (SPR) spectroscopy and quartz crystal microbalance (QCM) are surface sensitive analytical techniques capable of real-time monitoring of biomolecular interactions. In this article we review our past work on the use of these two techniques for studying protein–DNA interactions, exemplified with estrogen receptors (ER) and their response elements (ERE). Various assay schemes have been developed for a comprehensive characterization of ER–ERE interactions in terms of sequence specificity, binding affinity, stoichiometry, ligand effects on binding dynamics and conformational changes in the proteins and DNA. These are all important characteristics underlining the mechanism of ER-mediated gene transcription. With these studies we have made the following demonstrations to describe the advantages of these two techniques, namely (i) SPR technique is superior and more versatile than conventional (electrophoretic mobility shift assay) EMSA for studying protein-DNA interactions; (ii) QCM is an alternative tool for studying conformational changes in protein–DNA complexes and (iii) combinational SPR and QCM analysis provides additional characterization of biomolecular films, e.g. film thickness, water content, and conformation rigidity etc.

Sign in / Sign up

Export Citation Format

Share Document