ArticleThe journal of physical chemistry letters2015
Characterization of Parallel β-Sheets at Interfaces by Chiral Sum Frequency Generation Spectroscopy.
Article in The journal of physical chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Distinct adsorption behavior and structures of cell-penetrating peptides at a model lipid membrane interface: a heterodyne-detected vibrational sum frequency generation spectroscopy study.Chemical science · 2026Article
- Elevated concentrations cause upright alpha-synuclein conformation at lipid interfaces.Nature communications · 2023Article
- The Dysferlin C2A Domain Binds PI(4,5)P2 and Penetrates Membranes.Journal of molecular biology · 2023Article
- Acidic pH Promotes Refolding and Macroscopic Assembly of Amyloid β (16-22) Peptides at the Air-Water Interface.The journal of physical chemistry letters · 2022Article
- Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Chiral Inversion of Amino Acids in Antiparallel β-Sheets at Interfaces Probed by Vibrational Sum Frequency Generation Spectroscopy.The journal of physical chemistry. B · 2019Article
- Nonlinear Optical Methods for Characterization of Molecular Structure and Surface Chemistry.Topics in catalysis · 2018Article
- Broad-Bandwidth Chiral Sum Frequency Generation Spectroscopy for Probing the Kinetics of Proteins at Interfaces.Langmuir : the ACS journal of surfaces and colloids · 2015Article
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Authors and funding
6 authors.
Funding
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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