ArticleLangmuir : the ACS journal of surfaces and colloids2017
Graphite-Templated Amyloid Nanostructures Formed by a Potential Pentapeptide Inhibitor for Alzheimer's Disease: A Combined Study of Real-Time Atomic Force Microscopy and Molecular Dynamics Simulations.
Article in Langmuir : the ACS journal of surfaces and colloids, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Biological applications of graphene-based nanomaterials in neurodegenerative diseases.Materials today. Bio · 2025Review
- Current Advancement and Future Prospects: Biomedical Nanoengineering.Current radiopharmaceuticals · 2024Review
- Dimensional effect of graphene nanostructures on cytoskeleton-coupled anti-tumor metastasis.Smart medicine · 2023Article
- Recent Experimental Advances in Characterizing the Self-Assembly and Phase Behavior of Polypeptoids.Materials (Basel, Switzerland) · 2023Review
- 3D AFM Nanomechanical Characterization of Biological Materials.Nanomaterials (Basel, Switzerland) · 2023Article
- Determining Spatial Variability of Elastic Properties for Biological Samples Using AFM.Micromachines · 2023Review
- Review
- Investigating and characterizing the binding activity of the immobilized calmodulin to calmodulin-dependent protein kinase I binding domain with atomic force microscopy.Chemistry Central journal · 2017Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Self-assembly of peptides is closely related to many diseases, including Alzheimer's, Parkinson's, and prion diseases. Understanding the basic mechanism of this assembly is essential for designing ultimate cure and preventive measures. Template-assisted self-assembly (TASA) of peptides on inorganic substrates can provide fundamental understanding of substrate-dependent peptides assemble, including the role of hydrophobic interface on the peptide fibrillization. Here, we have studied the self-assembly process of a potential pentapeptide inhibitor on the surface of highly oriented pyrolytic graphite (HOPG) using real time atomic force microscopy (RT-AFM) as well as molecular dynamics (MD) simulation. Experimental and simulation results show nanofilament formation consisting of β-sheet structures and epitaxial growth on HOPG. Height analysis of the nanofilaments and MD simulation indicate that the peptides adopt a lying down configuration of double-layered antiparallel β-sheets for its epitaxial growth, and the number of nanofilament layers is concentration-dependent. These findings provide new perspective for the mechanism of peptide-based fibrillization in amyloid diseases as well as for designing well-ordered micrometrical and nanometrical structures.
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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.