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Related Concept Videos

Pigmentation01:19

Pigmentation

The color of the skin is influenced by a number of pigments, including melanin, carotene, and hemoglobin. Recall that melanin is produced by cells called melanocytes, which are found scattered throughout the stratum basale of the epidermis. The melanin is transferred to the keratinocytes via melanosomes.
Melanin occurs in two primary forms: eumelanin that provides black and brown pigment and pheomelanin that provides red color. Dark-skinned individuals produce more melanin than those with pale...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...
Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

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Related Experiment Video

Updated: May 19, 2026

Laser Microdissection-Based Protocol for the LC-MS/MS Analysis of the Proteomic Profile of Neuromelanin Granules
07:35

Laser Microdissection-Based Protocol for the LC-MS/MS Analysis of the Proteomic Profile of Neuromelanin Granules

Published on: December 16, 2021

Eumelanin fibrils.

Ross McQueenie1, Jens Sutter, Jan Karolin

  • 1University of Strathclyde, Department of Physics, Photophysics Group, Centre for Molecular Nanometrology, SUPA, Glasgow, G4 0NG, Scotland.

Journal of Biomedical Optics
|August 17, 2012
PubMed
Summary
This summary is machine-generated.

Researchers synthesized eumelanin fibrils from L-DOPA auto-oxidation. These self-assembled structures mimic natural melanin and offer insights into its function and potential applications in materials science and medicine.

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Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens
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Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens

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Last Updated: May 19, 2026

Laser Microdissection-Based Protocol for the LC-MS/MS Analysis of the Proteomic Profile of Neuromelanin Granules
07:35

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Published on: December 16, 2021

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens
06:08

Preparation and Immunofluorescence Staining of Bundles and Single Fiber Cells from the Cortex and Nucleus of the Eye Lens

Published on: June 9, 2023

Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Biophysics

Background:

  • Eumelanin, a natural pigment, has unique photophysical properties.
  • Understanding eumelanin's structure is crucial for its applications.
  • 3, 4-dihydroxy-L-phenylalanine (L-DOPA) is a precursor to melanin.

Purpose of the Study:

  • To describe the spontaneous formation of eumelanin fibrils from L-DOPA.
  • To characterize the structure and properties of these synthetic fibrils.
  • To explore potential applications of synthetic eumelanin.

Main Methods:

  • Auto-oxidation of L-DOPA followed by drying.
  • Characterization using scanning electron microscopy (SEM) and atomic force microscopy (AFM).
  • Spectroscopic analysis including fluorescence spectroscopy and fluorescence lifetime imaging microscopy (FLIM).

Main Results:

  • Spontaneous formation of unidirectional eumelanin fibrils (∼1–2 μm diameter) upon drying.
  • Fibrils exhibit core eumelanin with efficient nonradiative decay, alongside pockets of radiative species.
  • Branches formed at specific angles (20–22 deg); occasional solution fibrils attributed to microbial scaffolds.

Conclusions:

  • Synthetic eumelanin fibrils can be fabricated via L-DOPA auto-oxidation.
  • These fibrils mimic natural melanin's properties, offering a model for functional structure studies.
  • Potential applications include novel materials and understanding L-DOPA's role in Parkinson's disease treatment.