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

Protein Folding

Protein Folding

Protein and Protein Structure

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

Detergent Purification of Membrane Proteins

Detergent Purification of Membrane Proteins

Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...

Protein Denaturation

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

You might also read

Related Articles

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

Sort by

Same author

[Polymorphisms of five short tandem repeat systems in Chinese Han population in Chengdu].

Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics·2000

Same author

Microinfusion of protein kinase inhibitor H7 into the cerebellum impairs the acquisition but not the retention of classical eyeblink conditioning in rabbits.

Brain research·2000

Same author

Role of climbing fibers in determining the spatial patterns of activation in the cerebellar cortex to peripheral stimulation: an optical imaging study.

Neuroscience·2000

Same author

[Experimental study on hypoglycemic effect of YTY granules].

Hunan yi ke da xue xue bao = Hunan yike daxue xuebao = Bulletin of Hunan Medical University·2000

Same author

[Comparative study of left ventricular morphology and function of patients with left ventricular systolic and diastolic heart failure on echocardiography].

Hunan yi ke da xue xue bao = Hunan yike daxue xuebao = Bulletin of Hunan Medical University·2000

Same author

[Clinical study on left ventricular diastolic heart failure in the aged patients].

Hunan yi ke da xue xue bao = Hunan yike daxue xuebao = Bulletin of Hunan Medical University·2000

Search research articles

Related Experiment Video

Updated: Jul 11, 2026

Synthesis of Soft Polysiloxane-urea Elastomers for Intraocular Lens Application

Synthesis of Soft Polysiloxane-urea Elastomers for Intraocular Lens Application

Published on: March 8, 2019

Protein denaturation induced by cyclic silicone

L Sun¹, H Alexander, N Lattarulo

¹Department of Bioengineering, Hospital for Joint Diseases, Orthopaedic Institute, New York, NY 10003, USA.

|June 5, 1998

Summary

Octamethylcyclotetrasiloxane (D4) causes protein denaturation and conformational changes in fibronectin and fibrinogen in vitro. This may explain how silicones can trigger an immune response, potentially leading to autoimmune diseases.

More Related Videos

Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

Published on: January 7, 2019

Improved Polydimethylsiloxane (PDMS) Double Casting via Silicone Oil Treatment for Densely Packed Microstructure Replication

Improved Polydimethylsiloxane (PDMS) Double Casting via Silicone Oil Treatment for Densely Packed Microstructure Replication

Published on: July 18, 2025

Related Experiment Videos

Last Updated: Jul 11, 2026

Synthesis of Soft Polysiloxane-urea Elastomers for Intraocular Lens Application

Synthesis of Soft Polysiloxane-urea Elastomers for Intraocular Lens Application

Published on: March 8, 2019

Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

Drawing and Hydrophobicity-patterning Long Polydimethylsiloxane Silicone Filaments

Published on: January 7, 2019

Improved Polydimethylsiloxane (PDMS) Double Casting via Silicone Oil Treatment for Densely Packed Microstructure Replication

Improved Polydimethylsiloxane (PDMS) Double Casting via Silicone Oil Treatment for Densely Packed Microstructure Replication

Published on: July 18, 2025

Area of Science:

Biochemistry
Immunology
Materials Science

Background:

Low-molecular-weight cyclic silicones, such as octamethylcyclotetrasiloxane (D4), are known to have adjuvant activity.
The precise mechanism by which silicones elicit an immunological response remains unclear.

Purpose of the Study:

To investigate the in vitro effects of D4 on protein structure.
To explore the potential link between D4-induced protein changes and autoimmune responses.

Main Methods:

Utilized fluorescence spectroscopy to detect changes in protein fluorescence intensity and wavelength shifts.
Employed circular dichroism (CD) spectroscopy to assess alterations in protein secondary and tertiary structures.
Incubated fibronectin (Fn) and fibrinogen (Fbg) with D4 at varying concentrations and durations.

Main Results:

D4 induced significant denaturation and aggregation of Fn and Fbg, evidenced by protein precipitation.
Fluorescence spectroscopy revealed decreased intensity and red-shifted emission maxima, indicating protein unfolding.
CD spectral analysis confirmed conformational changes in the proteins upon exposure to D4.

Conclusions:

D4 directly causes denaturation and conformational alterations in key proteins like Fn and Fbg.
These D4-induced protein modifications may function as neoantigens, stimulating an immune response.
The findings suggest a potential pathway for silicone-induced autoimmunity.