Plasmon Waveguide Resonance Spectroscopy: Principles and Applications in Studies of Molecular Interactions within Membranes

2015 ◽  
pp. 89-118 ◽  
Author(s):  
Isabel Alves
Biochemistry ◽  
2006 ◽  
Vol 45 (16) ◽  
pp. 5309-5318 ◽  
Author(s):  
Isabel D. Alves ◽  
Diane Delaroche ◽  
Bernard Mouillac ◽  
Zdzislaw Salamon ◽  
Gordon Tollin ◽  
...  

2004 ◽  
Vol 65 (5) ◽  
pp. 1248-1257 ◽  
Author(s):  
Isabel D. Alves ◽  
Scott M. Cowell ◽  
Zdzislaw Salamon ◽  
Savitha Devanathan ◽  
Gordon Tollin ◽  
...  

Author(s):  
Gil U Lee ◽  
Linda Chrisey ◽  
Richard J. Colton

Structure and function in biological macromolecular systems such as proteins and polynucleotides are based on intermolecular interactions that are short ranged and chemically specific. Our knowledge of these molecular interactions results from indirect physical and thermodynamic measurements such as x-ray crystallography, light scattering and nuclear magnetic resonance spectroscopy. Direct measurement of molecular interaction forces requires that the state of a system be monitored with near atomic resolution while an independent force is applied to the system of 10−12 to 10−9 Newton magnitude. The atomic force microscope (AFM) has recently been applied to the study of single molecular interactions. The microfabricated cantilever of the AFM, a force transducer of small yet variable stiffness and high resonance frequency, produces a transducer of 10−15 N/Hz1/2 force sensitivities and 0.01 nm position accuracy.This presentation describes the AFM measurement of the molecular interaction forces in the model ligand-receptor system streptavidin-biotin and between complementary strands of DNA.


2005 ◽  
Vol 77 (8) ◽  
pp. 2569-2574 ◽  
Author(s):  
Savitha Devanathan ◽  
Zdzislaw Salamon ◽  
Anoop Nagar ◽  
Subhash Narang ◽  
Donald Schleich ◽  
...  

1999 ◽  
Vol 24 (6) ◽  
pp. 213-219 ◽  
Author(s):  
Zdzislaw Salamon ◽  
Michael F. Brown ◽  
Gordon Tollin

2009 ◽  
Vol 63 (9) ◽  
pp. 1062-1067 ◽  
Author(s):  
Han Zhang ◽  
Kristina S. Orosz ◽  
Hiromi Takahashi ◽  
S. Scott Saavedra

A commercially available spectrometer has been modified to perform plasmon waveguide resonance (PWR) spectroscopy over a broad spectral bandwidth. When compared to surface plasmon resonance (SPR), PWR has the advantage of allowing measurements in both s- and p-polarizations on a waveguide surface that is silica or glass rather than a noble metal. Here the waveguide is a BK7 glass slide coated with silver and silica layers. The resonance wavelength is sensitive to the optical thickness of the medium adjacent to the silica layer. The sensitivity of this technique is characterized and compared with broadband SPR both experimentally and theoretically. The sensitivity of spectral PWR is comparable to that of spectral SPR for samples with refractive indices close to that of water. The hydrophilic surface of the waveguide allows supported lipid bilayers to be formed spontaneously by vesicle fusion; in contrast, the surface of an SPR chip requires chemical modification to create a supported lipid membrane. Broadband PWR spectroscopy should be a useful technique to study biointerfaces, including ligand binding to transmembrane receptors and adsorption of peripheral proteins on ligand-bearing membranes.


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