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

Autor: Fu L; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Wang Z; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Psciuk BT; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Xiao D; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Batista VS; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States., Yan EC; Department of Chemistry, Yale University, 225 Prospect Street, New Haven, Connecticut 06520, United States.
Jazyk: angličtina
Zdroj: The journal of physical chemistry letters [J Phys Chem Lett] 2015 Apr 16; Vol. 6 (8), pp. 1310-5. Date of Electronic Publication: 2015 Mar 27.
DOI: 10.1021/acs.jpclett.5b00326
Abstrakt: 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.
Databáze: MEDLINE