ArticleBiophysical chemistry2015
Conformational dynamics and aggregation behavior of piezoelectric diphenylalanine peptides in an external electric field.
Article in Biophysical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- Piezoelectric amino acids and peptides: Mechanisms, molecular engineering, and biomedical applications.iScience · 2026Review
- Design and Manufacturing of Piezoelectric Biomaterials for Bioelectronics and Biomedical Applications.Chemical reviews · 2025Review
- Non-Uniform Electric Field Manipulation of Chromogenic Peptide Amphiphile Assemblies.ChemSystemsChem · 2025Article
- Biodegradable Piezoelectric Polymers: Recent Advancements in Materials and Applications.Advanced healthcare materials · 2023Review
- Peptide-based nanomaterials: Self-assembly, properties and applications.Bioactive materials · 2022Review
- Replica Exchange Molecular Dynamics of Diphenylalanine Amyloid Peptides in Electric Fields.The journal of physical chemistry. B · 2021Article
- Invasive and non-invasive therapies for Alzheimer's disease and other amyloidosis.Biophysical reviews · 2020Review
- Modulation of aggregation with an electric field; scientific roadmap for a potential non-invasive therapy against tauopathies.RSC advances · 2019Article
- Conformational analysis of replica exchange MD: Temperature-dependent Markov networks for FF amyloid peptides.The Journal of chemical physics · 2018Article
- Modulation of Peptide Based Nano-Assemblies with Electric and Magnetic Fields.Scientific reports · 2017Article
- Thermal and aqueous stability improvement of graphene oxide enhanced diphenylalanine nanocomposites.Science and technology of advanced materials · 2017Article
- Self-assembly of diphenylalanine peptide with controlled polarization for power generation.Nature communications · 2016Article
- Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.Chemical communications (Cambridge, England) · 2016Article
- The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine.Molecules (Basel, Switzerland) · 2015Review
- Modulation of Alzheimer's Aβ protofilament-membrane interactions by lipid headgroups.ACS chemical neuroscience · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Aromatic peptides including diphenylalanine (FF) have the capacity to self-assemble into ordered, biocompatible nanostructures with piezoelectric properties relevant to a variety of biomedical applications. Electric fields are commonly applied to align FF nanotubes, yet little is known about the effect of the electric field on the assembly process. Using all-atom molecular dynamics with explicit water molecules, we examine the response of FF monomers to the application of a constant external electric field over a range of intensities. We probe the aggregation mechanism of FF peptides, and find that the presence of even relatively weak fields can accelerate ordered aggregation, primarily by facilitating the alignment of individual molecular dipole moments. This is modulated by the conformational response of individual FF peptides (e.g., backbone stretching) and by the cooperative alignment of neighboring FF and water molecules. These observations may facilitate future studies on the controlled formation of nanostructured aggregates of piezoelectric peptides and the understanding of their electro-mechanical properties.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.