ArticleBiophysical journal2022
Investigating the effects of N-terminal acetylation on KFE8 self-assembly with 2D IR spectroscopy.
Article in Biophysical journal, 2022. 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.
- Amphipathic β‑Sheet-Forming Octapeptide Self-Assembly Using the Martini Potential Family.ACS omega · 2026Article
- Stereoselective Coassembly of Chiral Isomer Peptide Pairs.ACS materials Au · 2026Article
- Advances in Probing Amyloid Heterogeneity Using Vibrational Spectroscopy and Imaging.The journal of physical chemistry. B · 2025Review
- Transition Dipole Strength as a Quantitative Tool for Protein Secondary Structure Analysis.The journal of physical chemistry. B · 2025Article
- Suppressing sidechain modes and improving structural resolution for 2D IR spectroscopy via vibrational lifetimes.The Journal of chemical physics · 2024Article
- Resolving the Nanoscale Structure of β-Sheet Peptide Self-Assemblies Using Single-Molecule Orientation-Localization Microscopy.ACS nano · 2024Article
- Probing local changes to α-helical structures with 2D IR spectroscopy and isotope labeling.Biophysical journal · 2023Article
- Determining the impact of gold nanoparticles on amyloid aggregation with 2D IR spectroscopy.The Journal of chemical physics · 2023Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide self-assembly is an exciting and robust approach to create novel nanoscale materials for biomedical applications. However, the complex interplay between intra- and intermolecular interactions in peptide aggregation means that minor changes in peptide sequence can yield dramatic changes in supramolecular structure. Here, we use two-dimensional infrared spectroscopy to study a model amphiphilic peptide, KFE8, and its N-terminal acetylated counterpart, AcKFE8. Two-dimensional infrared spectra of isotope-labeled peptides reveal that AcKFE8 aggregates comprise two distinct β-sheet structures although KFE8 aggregates comprise only one of these structures. Using an excitonic Hamiltonian to simulate the vibrational spectra of model β-sheets, we determine that the spectra are consistent with antiparallel β-sheets with different strand alignments, specifically a two-residue shift in the register of the β-strands. These findings bring forth new insights into how N-terminal acetylation may subtly impact secondary structure, leading to larger effects on overall aggregate morphology. In addition, these results highlight the importance of understanding the residue-level structural differences that result from changes in peptide sequence to facilitate the rational design of peptide materials.
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