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Related Experiment Video

Updated: Oct 2, 2025

Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α

Development and Validation of an Ultrasensitive Single Molecule Array Digital Enzyme-linked Immunosorbent Assay for Human Interferon-α

Published on: June 14, 2018

Interferon-β Activity Is Affected by S100B Protein.

Alexey S Kazakov¹, Alexander D Sofin¹, Nadezhda V Avkhacheva¹

¹Institute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institutskaya Str., 7, Pushchino, 142290 Moscow, Russia.

International Journal of Molecular Sciences

|February 26, 2022

Summary

This summary is machine-generated.

Interferon-beta (IFN-β) interacts with S100B protein, influencing its activity. This interaction, particularly with monomeric S100B, significantly enhances IFN-β binding and affects cell viability, suggesting roles in disease progression.

Keywords:

S100B cancer cytokine interferon neurological diseases protein–protein interaction

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Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

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Published on: September 29, 2019

Area of Science:

Biochemistry
Molecular Biology
Immunology

Background:

Interferon-beta (IFN-β) is a cytokine used therapeutically but its full potential is limited by poorly understood regulatory mechanisms.
Previous research identified interactions between IFN-β and several S100 proteins (S100A1, S100A4, S100A6, S100P), which are calcium-binding proteins with cytokine-like properties.
S100B protein is implicated in various oncological and neurological diseases.

Purpose of the Study:

To investigate the interaction between Interferon-beta (IFN-β) and the S100B protein.
To characterize the binding kinetics and affinity of the IFN-β/S100B complex.
To assess the functional consequences of the IFN-β/S100B interaction on cancer cell viability.

Main Methods:

Chemical crosslinking
Intrinsic fluorescence spectroscopy
Surface plasmon resonance (SPR) spectroscopy
Crystal violet cell viability assay
Bioinformatics analysis

Main Results:

IFN-β binds to both dimeric and monomeric forms of calcium-bound S100B.
Calcium depletion abolishes the interaction between S100B and IFN-β.
Monomerization of S100B dramatically increases its affinity for IFN-β (equilibrium dissociation constant of 47 pM).
Co-application of IFN-β and S100B neutralized their inhibitory effects on MCF-7 cell viability.
Bioinformatics suggests S100B modulation of IFN-β activity is relevant to oncological and neurological diseases.

Conclusions:

S100B directly interacts with IFN-β, modulating its activity.
The affinity of S100B for IFN-β is highly dependent on calcium binding and S100B oligomeric state.
The interaction between IFN-β and S100B has functional implications for cell viability and potentially disease progression in cancer and neurological disorders.