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Fibrous Proteins

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...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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Mechanism of Filopodia Formation

Mechanism of Filopodia Formation

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Disassembly of Intermediate Filaments

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Actin Polymerization

Actin Polymerization

Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
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Globular and Fibrous Proteins

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Related Experiment Video

Updated: May 16, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

Published on: August 13, 2014

Fibril formation by pH and temperature responsive silk-elastin block copolymers.

Monika D Golinska¹, Thao T H Pham, Marc W T Werten

¹Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, NL-6703 HB Wageningen, The Netherlands.

Biomacromolecules

|December 11, 2012

Summary

Silk-elastin-like proteins self-assemble into fibrils. Elastin-like blocks influence fibril length and cause temperature-dependent aggregation, impacting material properties.

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Last Updated: May 16, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications

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Published on: August 13, 2014

Silk Film Culture System for in vitro Analysis and Biomaterial Design

Silk Film Culture System for in vitro Analysis and Biomaterial Design

Published on: April 24, 2012

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Published on: August 13, 2019

Area of Science:

Biomaterials Science
Polymer Chemistry
Protein Engineering

Background:

Silk-elastin-like proteins (SELPs) are engineered biomaterials with tunable properties.
Understanding their self-assembly is crucial for developing advanced materials.

Purpose of the Study:

To investigate the self-assembly behavior of two distinct SELP architectures: S(24)E(40) and S(12)C(4)E(40).
To elucidate the role of elastin-like blocks in fibril formation and material properties.

Main Methods:

Synthesis and characterization of silk-elastin-like protein diblock (S(24)E(40)) and triblock (S(12)C(4)E(40)) copolymers.
pH-induced self-assembly studies and analysis of fibril nucleation and growth kinetics.
Temperature-dependent rheological measurements to assess material properties.

Main Results:

Lowering pH triggers self-assembly of acidic silk-like blocks into fibrils via nucleation-and-growth.
Elastin-like blocks promote homogeneous nucleation, leading to polydisperse fibril lengths and concentration-dependent growth.
Elastin-like blocks introduce temperature sensitivity, causing irreversible fibril aggregation and loss of elasticity at elevated temperatures.

Conclusions:

SELP architecture significantly impacts self-assembly mechanisms and resulting fibril characteristics.
The incorporation of elastin-like blocks provides a mechanism for controlling fibril length and introduces thermo-responsive aggregation behavior.
These findings offer insights into designing responsive biomaterials with tunable mechanical properties.