ArticleRSC advances2019
Self-assembly of l-phenylalanine amino acid: electrostatic induced hindrance of fibril formation.
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 65 citations in OpenAlex.
- Self-assembled metabolite-derived amyloid-like structures: implications for disease, therapeutics, and biomedical applications.Molecular biology reports · 2026Review
- Unveiling the phenylalanine coaggregation mechanism for a deep understanding of phenylketonuria disease.Scientific reports · 2025Article
- Co-MoOMaterials (Basel, Switzerland) · 2025Article
- Spectroscopic Investigation of Hydrogels Formed from Phenylalanine.Journal of fluorescence · 2025Article
- Micropatterning Photoconductive Peptide Assemblies on Stiff and Soft Biomaterial Substrates.ACS applied materials & interfaces · 2025Article
- Nanometric and Hydrophobic Green Rust Minerals upon Exposure to Amino Acids and Nickel as Prerequisites for a Primitive Chemiosmosis.Life (Basel, Switzerland) · 2025Article
- Ordered Aggregates of Fmoc-Diphenylalanine at Alkaline pH as a Precursor of Fibril Formation and Peptide Gelation.The journal of physical chemistry. B · 2025Article
- Preparation of Gelatin-Quaternary Ammonium Salt Coating on Titanium Surface for Antibacterial/Osteogenic Properties.Molecules (Basel, Switzerland) · 2023Article
- Antibacterial and Cytocompatible pH-Responsive Peptide Hydrogel.Molecules (Basel, Switzerland) · 2023Article
- Enhancing Photothermal Therapy Efficacy byACS applied materials & interfaces · 2023Review
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Article
- Insights into the Thermally Activated Cyclization Mechanism in a Linear Phenylalanine-Alanine Dipeptide.The journal of physical chemistry. B · 2022Article
- Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.Frontiers in bioengineering and biotechnology · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nanostructure morphology originating from the self-assembly of molecules has attracted substantial attention due to its role in toxic amyloid fibril formation and immense potential in the design and fabrication of novel biomaterials. This study presents the role of intermolecular electrostatic interaction on the self-assembly process of l-phenylalanine (L-Phe) amino acid. We have employed attenuated total reflection Fourier transform infrared spectroscopy to probe the existence of different ionization states of the amino acid in various pH aqueous solutions. The self-assembly process of L-Phe in the aqueous phase is explored by using circular dichroism absorption and nuclear magnetic resonance spectroscopic tools. The observed spectral features have shown the signature of higher order structures and possible perturbation in the π-π stacking aromatic interactions for the cationic and anionic states of the amino acid. Scanning electron microscopy is used to probe the self-assembled morphology of the L-Phe amino acid dried samples prepared from the same pH aqueous solutions. We find that for the case of zwitterionic states the self-assembly nanostructures are dominated by the presence of fibrillar morphology, however interestingly for cationic and anionic states the morphology is dominated by the presence of flakes. Our finding demonstrates the potential influence of intermolecular electrostatic interaction over the aromatic π-π stacking interaction in hindering the fibril formation.
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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.