Gold-SPIDER: spectral phase interferometry for direct electric field reconstruction utilizing sum-frequency generation from a gold surface

2008 ◽  
Vol 25 (6) ◽  
pp. A13 ◽  
Author(s):  
Matthew E. Anderson ◽  
Tobias Witting ◽  
Ian A. Walmsley
Author(s):  
Chiho Katagiri ◽  
Takayuki Miyamae ◽  
Hao Li ◽  
Fangyuan Yang ◽  
Steven Baldelli

Sum frequency generation imaging microscopy was applied to visualize the internal electric-field behavior in operating organic field effect transistors.


2015 ◽  
Vol 177 ◽  
pp. 493-505 ◽  
Author(s):  
Ayanjeet Ghosh ◽  
Jia-Jung Ho ◽  
Arnaldo L. Serrano ◽  
David R. Skoff ◽  
Tianqi Zhang ◽  
...  

By adding a mid-infrared pulse shaper to a sum-frequency generation (SFG) spectrometer, we have built a 2D SFG spectrometer capable of measuring spectra analogous to 2D IR spectra but with monolayer sensitivity and SFG selection rules. In this paper, we describe the experimental apparatus and provide an introduction to 2D SFG spectroscopy to help the reader interpret 2D SFG spectra. The main aim of this manuscript is to report 2D SFG spectra of the amyloid forming peptide FGAIL. FGAIL is a critical segment of the human islet amyloid polypeptide (hIAPP or amylin) that aggregates in people with type 2 diabetes. FGAIL is catalyzed into amyloid fibers by many types of surfaces. Here, we study the structure of FGAIL upon deposition onto a gold surface covered with a self-assembled monolayer of methyl-4-mercaptobenzoate (MMB) that produces an ester coating. FGAIL deposited on bare gold does not form ordered layers. The measured 2D SFG spectrum is consistent with amyloid fiber formation, exhibiting both the parallel (a+) and perpendicular (a−) symmetry modes associated with amyloid β-sheets. Cross peaks are observed between the ester stretches of the coating and the FGAIL peptides. Simulations are presented for two possible structures of FGAIL amyloid β-sheets that illustrate the sensitivity of the 2D SFG spectra to structure and orientation. These results provide some of the first molecular insights into surface catalyzed amyloid fiber structure.


2012 ◽  
Vol 27 ◽  
pp. 571-579 ◽  
Author(s):  
Emilie Bulard ◽  
Marie-Pierre Fontaine-Aupart ◽  
Henri Dubost ◽  
Wanquan Zheng ◽  
Jean-Marie Herry ◽  
...  

In biomedical and food industry, surface colonization by bacteria is harmful: it leads to biofilm formation, a microbial consortia more resistant to antibiotics than planktonic bacteria. In order to design materials able to limit the biofilm formation, the effect of bacteria on materials has to be well characterized. In this work, a well-defined surface composed of a self-assembled monolayer (SAM) of octadecanethiol (ODT) onto a gold surface is probedin situ. The SAM conformation is obtained using the femtosecond vibrational sum frequency generation (SFG) spectroscopy. This technique provides selectively the molecular vibrational signature of the interface. The behaviour of the ODT SAM is studied in different environments: in air, in water, and upon exposure to hydrophilic or hydrophobicLactococcus lactisbacteria. Modelling the experimental SFG spectra reveals a measurable change of the SAM conformation which depends on the environment, especially on the hydrophilic-hydrophobic character.


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