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Generalizable Protein Biosensors Based on Synthetic Switch Modules.

Zhong Guo1, Wayne A Johnston1, Jason Whitfield2

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Summary
This summary is machine-generated.

Scientists engineered versatile protein switches for synthetic biology. These peptide-controlled systems enable precise regulation of biological functions and accurate detection of clinical biomarkers, opening new avenues for biosensing applications.

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Area of Science:

  • Synthetic biology
  • Protein engineering
  • Biosensing

Background:

  • Allosteric protein switches are crucial for biological information processing.
  • Engineered allosteric switches are desirable tools for synthetic systems.

Purpose of the Study:

  • To develop a general strategy for creating peptide-operated synthetic allosteric ON switches.
  • To demonstrate the conversion of constitutively active enzymes into controllable switches.

Main Methods:

  • Insertion of a calmodulin domain into rationally selected sites of enzymes.
  • Engineering activator peptides to modulate switch activity via ligand-mediated proximity.
  • Utilizing created biosensors for analyte detection in biological fluids.

Main Results:

  • Successfully converted enzymes (EGFP, glucose dehydrogenase, NanoLuciferase, dehydrofolate reductase) into peptide-switches with minimal optimization.
  • Achieved dynamic response ranges from 1.8-fold to over 200-fold.
  • Demonstrated accurate measurement of clinical drugs and biomarkers in plasma, saliva, and urine.

Conclusions:

  • The presented strategy provides a generalizable method for constructing efficient protein switches.
  • These switches enable the conversion of analyte binding into desired biochemical activity.
  • The approach facilitates the creation of complex artificial signaling and metabolic circuits.