ArticleNature communications2019
Self-assembling peptides imaged by correlated liquid cell transmission electron microscopy and MALDI-imaging mass spectrometry.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Who cites it
20 citing papers in PubMed.
- Ultrathin liquid cells for microsecond time-resolved cryo-EM.Nature communications · 2026Article
- Probing Peptide Assembly and Interaction via High-Resolution Imaging Techniques: A Mini Review.International journal of molecular sciences · 2025Review
- Evaluation of combined workflows for multimodal mass spectrometry imaging of elements and lipids from the same tissue section.Analytical and bioanalytical chemistry · 2025Article
- Surface Functionalization of Elastomers with Biopolymers.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Understanding, Mimicking, and Mitigating Radiolytic Damage to Polymers in Liquid Phase Transmission Electron Microscopy.Advanced materials (Deerfield Beach, Fla.) · 2024Article
- Nanopipette dynamic microscopy unveils nano coffee ring.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Upper critical solution temperature polymer assemblies via variable temperature liquid phase transmission electron microscopy and liquid resonant soft X-ray scattering.Nature communications · 2023Article
- Ouzo Effect Examined at the Nanoscale via Direct Observation of Droplet Nucleation and Morphology.ACS central science · 2023Article
- Direct Imaging of the Kinetic Crystallization Pathway: Simulation and Liquid-Phase Transmission Electron Microscopy Observations.Materials (Basel, Switzerland) · 2023Review
- Supramolecular systems chemistry through advanced analytical techniques.Analytical and bioanalytical chemistry · 2022Review
- Coordination Cage-Based Emulsifiers: Templated Formation of Metal Oxide Microcapsules Monitored by In Situ LC-TEM.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Multi-step atomic mechanism of platinum nanocrystals nucleation and growth revealed by in-situ liquid cell STEM.Scientific reports · 2021Article
- Thermoresponsive polymer assemblies via variable temperature liquid-phase transmission electron microscopy and small angle X-ray scattering.Nature communications · 2021Article
- Dipeptide Nanostructure Assembly and DynamicsACS nano · 2021Article
- Cell-Instructive Surface Gradients of Photoresponsive Amyloid-like Fibrils.ACS biomaterials science & engineering · 2021Article
- From structure to application: Progress and opportunities in peptide materials development.Current opinion in chemical biology · 2021Review
- Emergence and Rearrangement of Dynamic Supramolecular Aggregates Visualized by Interferometric Scattering Microscopy.ACS nano · 2020Article
- Article
- UV-responsive cyclic peptide progelator bioinks.Faraday discussions · 2019Article
- Advances in mass spectrometry imaging for spatial cancer metabolomics.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We describe the observation of stimuli-induced peptide-based nanoscale assemblies by liquid cell transmission electron microscopy (LCTEM). LCTEM offers the opportunity to directly image nanoscale materials in liquid. Despite broad interest in characterizing biological phenomena, electron beam-induced damage remains a significant problem. Concurrently, methods for verifying chemical structure during or following an LCTEM experiment have been few, with key examples limited to electron diffraction or elemental analysis of crystalline materials; this strategy is not translatable to biopolymers observed in nature. In this proof-of-concept study, oligomeric peptides are biologically or chemically stimulated within the liquid cell in a TEM to assemble into nanostructures. The resulting materials are analyzed by MALDI-imaging mass spectrometry (MALDI-IMS) to verify their identity. This approach confirms whether higher-order assemblies observed by LCTEM consist of intact peptides, verifying that observations made during the in situ experiment are because of those same peptides and not aberrant electron beam damage effects.
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