Characterization of Parallel β-Sheets at Interfaces by Chiral Sum Frequency Generation Spectroscopy

Document Type

Article

Publication Date

2015

MeSH Terms

Islet Amyloid Polypeptide, Spectrum Analysis

Subject: LCSH

Amylin, Spectrum analysis

Disciplines

Chemical Engineering | Chemistry

Abstract

Characterization of protein secondary structures at interfaces is still challenging due to the limitations of surface-selective optical techniques. Here, we address the challenge of characterizing parallel β-sheets by combining chiral sum frequency generation (SFG) spectroscopy and computational modeling. We focus on human islet amyloid polypeptide aggregates and a de novo designed short polypeptide at lipid/water and air/glass interfaces. We find that parallel β-sheets adopt distinct orientations at various interfaces and exhibit characteristic chiroptical responses in the amide I and N–H stretch regions. Theoretical analysis indicates that the characteristic chiroptical responses provide valuable information on the symmetry, orientation, and vibrational couplings of parallel β-sheet at interfaces.

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DOI

10.1021/jp307406j

Publisher Citation

Fu, L., Wang, Z., Psciuk, B. T., Xiao, D., Batista, V. S., & Yan, E. C. Y. (2015). Characterization of Parallel β-Sheets at Interfaces by Chiral Sum Frequency Generation Spectroscopy. The Journal of Physical Chemistry Letters, 6(8), 1310–1315.

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