# Engineered Protein Modification: A New Paradigm for Enhancing Biosensing Sensitivity and Diagnostic Accuracy

**Authors:** Zheng Xu, Chu Wang, Ziting Zhang, Heng Wang, Peiyi Gao, Lixing Weng

PMC · DOI: 10.3390/bios16010021 · Biosensors · 2025-12-26

## TL;DR

This paper reviews how engineered protein modifications can improve biosensor performance for better diagnostics and disease detection.

## Contribution

The novelty lies in systematically analyzing how engineered post-translational modifications enhance biosensing technologies.

## Key findings

- Strategic manipulation of PTMs improves biosensor sensitivity and specificity.
- Significant advancements in detection platforms have been identified.
- Persistent challenges remain in real-world integration and standardization.

## Abstract

Protein modifications, particularly post-translational modifications (PTMs) such as phosphorylation and glycosylation, are fundamental mechanisms regulating cellular activity and disease pathogenesis, with their detection emerging as a promising frontier for advanced diagnostics. This review systematically examines the integration of engineered protein modifications with biosensing technologies to enhance analytical performance and diagnostic accuracy. Through critical analysis of current methodologies, we highlight how strategic manipulation of PTMs improves biosensor sensitivity and specificity in applications ranging from early disease detection to environmental monitoring. The analysis identifies significant advancements in detection platforms while acknowledging persistent challenges in real-world integration and standardization. We conclude that optimizing protein modification-based sensing strategies represents a crucial pathway for developing robust, clinically translatable diagnostic tools, and propose focused research directions to address existing technical barriers and accelerate practical implementation.

## Full text

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## Figures

7 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12839059/full.md

## References

234 references — full list in the complete paper: https://tomesphere.com/paper/PMC12839059/full.md

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Source: https://tomesphere.com/paper/PMC12839059