Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Extracellular Vesicle-like Associated microRNAs in Monofloral Honeys: Molecular Characterization and Functional Pathways.

International journal of molecular sciences·2026

Same author

Peptide-Based pH-Responsive MRI-CEST Agents: In Vivo Comparison between a Selected Pentapeptide and the Established Iopamidol Reference in Tumor pH Mapping Ability.

Chemical & biomedical imaging·2026

Same author

Mechanically Enhanced Ultrashort Peptide Hydrogels for pH-Triggered Release.

ACS polymers Au·2026

Same author

Halogen-Controlled Aromatic Interactions Drive the Self-Assembly and Mechanics of Peptide Hydrogels.

ACS applied bio materials·2026

Same author

Poly-L-Lysine Doped FmocFF Nanogels as Delivery Platforms for siRNA.

ACS applied bio materials·2026

Same author

Peptide-Based Nanogels for Pharmaceutical and Biotechnological Applications: From Fmoc-FF to Other Peptide Sequences.

Pharmaceuticals (Basel, Switzerland)·2026

Search research articles

Related Experiment Video

Updated: Oct 21, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Fluorescence Emission of Self-assembling Amyloid-like Peptides: Solution versus Solid State.

Carlo Diaferia¹, Chiara Schiattarella², Enrico Gallo³

¹Department of Pharmacy and, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", Via Mezzocannone 16, Naples, 80134, Italy.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry

|September 8, 2021

Summary

The physical state of self-assembling amyloid-like peptides significantly alters their fluorescence. Solid-state amyloids show excitation-dependent emission, while solution-state peptides exhibit excitation-independent fluorescence.

Keywords:

amyloid fluorescence intrinsic fluorescence peptide materials self-assembly solid state

More Related Videos

Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging

Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging

Published on: March 27, 2020

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Related Experiment Videos

Last Updated: Oct 21, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging

Characterization of Amyloid Structures in Aging C. Elegans Using Fluorescence Lifetime Imaging

Published on: March 27, 2020

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

Biophysics
Materials Science
Spectroscopy

Background:

Amyloid peptides self-assemble into fibrillar structures with implications in various biological processes and diseases.
Understanding the photophysical properties of amyloid-like peptides is crucial for developing diagnostic and therapeutic tools.

Purpose of the Study:

To investigate the influence of physical state (solution vs. solid) on the UV-visible fluorescence of self-assembling amyloid-like peptides.
To characterize the excitation-dependent and independent fluorescence emission behaviors observed in different states.

Main Methods:

Analysis of intrinsic UV-visible fluorescence spectroscopy.
Comparison of fluorescence properties in solution and solid states.

Main Results:

A linear dependence of fluorescence emission peaks on excitation wavelength was observed in the solid state.
An excitation-independent fluorescence emission was detected for amyloid-like peptides in solution.
Significant differences in optical properties were highlighted based on the physical state.

Conclusions:

The physical state of amyloid-like peptides profoundly impacts their fluorescence emission characteristics.
These findings provide a critical benchmark for understanding amyloid fluorescence.
The study differentiates fluorescence behavior between solid-state and solution-state amyloid assemblies.