ArticleBiophysical journal2004
Self-assembly of the ionic peptide EAK16: the effect of charge distributions on self-assembly.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Self-Assembling Short Peptide Carriers for Gene Delivery.International journal of molecular sciences · 2026Review
- Biliary Injuries Repair Using Copolymeric Scaffold: A Systematic Review and In Vivo Experimental Study.Journal of functional biomaterials · 2025Article
- Unraveling the Atomistic Mechanism of Electrostatic Lateral Association of Peptide β-Sheet Structures and Its Role in Nanofiber Growth and Hydrogelation.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- DRGD-linked charged EKKE dimeric dodecapeptide: pH-based amyloid nanostructures and their application in lead and uranium binding.RSC advances · 2024Article
- Article
- Self-assembled nanoparticles: A new platform for revolutionizing therapeutic cancer vaccines.Frontiers in immunology · 2023Review
- Self-Assembling Peptides: From Design to Biomedical Applications.International journal of molecular sciences · 2021Review
- SERS Investigation on Oligopeptides Used as Biomimetic Coatings for Medical Devices.Biomolecules · 2021Article
- Chemically-Induced Cross-Linking of Peptidic Fibrils for Scaffolding Polymeric Particles and Macrophages.Macromolecular bioscience · 2021Article
- Self-Assembling Peptide Gels for 3D Prostate Cancer Spheroid Culture.Macromolecular bioscience · 2019Article
- RNA extraction from self-assembling peptide hydrogels to allow qPCR analysis of encapsulated cells.PloS one · 2018Article
- Promoting 3-D Aggregation of FACS Purified Thymic Epithelial Cells with EAK 16-II/EAKIIH6 Self-assembling Hydrogel.Journal of visualized experiments : JoVE · 2016Article
- Local retention of antibodies in vivo with an injectable film embedded with a fluorogen-activating protein.Journal of controlled release : official journal of the Controlled Release Society · 2016Article
- Rational design of fiber forming supramolecular structures.Experimental biology and medicine (Maywood, N.J.) · 2016Review
- Mechanisms of the self-assembly of EAK16-family peptides into fibrillar and globular structures: molecular dynamics simulations from nano- to micro-seconds.European biophysics journal : EBJ · 2015Article
- Peptide Hydrogels - Versatile Matrices for 3D Cell Culture in Cancer Medicine.Frontiers in oncology · 2015Review
- All-atom molecular dynamics study of EAK16 peptide: the effect of pH on single-chain conformation, dimerization and self-assembly behavior.European biophysics journal : EBJ · 2014Article
- End-to-end self-assembly of RADA 16-I nanofibrils in aqueous solutions.Biophysical journal · 2012Article
- Self-assembly of rationally designed peptides under two-dimensional confinement.Biophysical journal · 2010Article
- Interaction of an ionic complementary peptide with a hydrophobic graphite surface.Protein science : a publication of the Protein Society · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amphiphilic peptides suspended in aqueous solution display a rich set of aggregation behavior. Molecular-level studies of relatively simple amphiphilic molecules under controlled conditions are an essential step toward a better understanding of self-assembly phenomena of naturally occurring peptides/proteins. Here, we study the influence of molecular architecture and interactions on the self-assembly of model peptides (EAK16s), using both experimental and theoretical approaches. Three different types of EAK16 were studied: EAK16-I, -II, and -IV, which have the same amino acid composition but different amino acid sequences. Atomic force microscopy confirms that EAK16-I and -II form fibrillar assemblies, whereas EAK16-IV forms globular structures. The Fourier transform infrared spectrum of EAK16-IV indicates the possible formation of a beta-turn structure, which is not found in EAK16-I and -II. Our theoretical and numerical studies suggest the underlying mechanism behind these observations. We show that the hairpin structure is energetically stable for EAK16-IV, whereas the chain entropy of EAK16-I and -II favors relatively stretched conformations. Our combined experimental and theoretical approaches provide a clear picture of the interplay between single-chain properties, as determined by peptide sequences (or charge distributions), and the emerging structure at the nano (or more coarse-grained) level.
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