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2015 ; 177
(ä): 493-505
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Two-dimensional sum-frequency generation (2D SFG) spectroscopy: summary of
principles and its application to amyloid fiber monolayers
#MMPMID25611039
Ghosh A
; Ho JJ
; Serrano AL
; Skoff DR
; Zhang T
; Zanni MT
Faraday Discuss
2015[]; 177
(ä): 493-505
PMID25611039
show ga
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 ?-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 ?-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.