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Calmodulin-dependent Signaling

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

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Study on a Plasmonic Tilted Fiber Grating-Based Biosensor for Calmodulin Detection.

Xiaoyong Chen¹, Jie Jiang², Nan Zhang²

¹School of Electrical Engineering and Intelligentization, Dongguan University of Technology, Dongguan 523808, China.

|July 2, 2021

Summary

This summary is machine-generated.

We developed a novel biosensor using a plasmonic tilted fiber Bragg grating to detect calmodulin. This device achieved a low limit of detection (0.44 nM) for this important biomarker.

Keywords:

calmodulin fiber-optic biosensor limit of detection surface plasmonic resonance tilted fiber Bragg grating

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Area of Science:

Biochemistry and Biophysics
Nanotechnology and Materials Science
Biomedical Engineering

Background:

Calmodulin (CaM) is a crucial eukaryotic protein regulating cellular processes and enzyme activity.
Abnormal CaM levels are linked to metabolic and neurological disorders, necessitating accurate detection methods.
Existing detection methods may lack sensitivity or real-time capabilities.

Purpose of the Study:

To develop and demonstrate a novel plasmonic tilted fiber Bragg grating (TFBG)-based biosensor for sensitive and label-free detection of calmodulin.
To investigate the performance characteristics of the TFBG biosensor, including its limit of detection and response in different conditions.
To validate the biosensor's ability to detect calmodulin-protein interactions influenced by calcium ions.

Main Methods:

Fabrication of a biosensor utilizing an 18° TFBG coated with a 50 nm gold nanofilm.
Immobilization of transient receptor potential (TRP) channels onto the gold surface as bio-recognition elements for calmodulin.
Experimental validation of the biosensor's performance using calmodulin solutions and assessment of calcium ion influence.

Main Results:

The plasmonic TFBG biosensor achieved a limit of detection (LOD) of 0.44 nM for calmodulin.
Demonstrated that calmodulin-TRP channel interaction is significantly weaker in the absence of calcium ions, aligning with biological expectations.
The biosensor exhibited a simple structure, ease of manufacturing, and small size.

Conclusions:

The proposed plasmonic TFBG biosensor offers a promising platform for sensitive, real-time, label-free detection of calmodulin.
The biosensor's design is suitable for microliter-volume biomolecule detection in various biochemical applications.
This technology has potential for clinical diagnostics and biochemical research requiring precise calmodulin quantification.