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Revealing Single-Amino Acid Recognition and Cleavage Dynamics Using Plasmonic Biosensors
Shaopeng Chang1, Xiaojing Sheng2, Yuqing Deng2
1Center for High Pressure Science, State Key Lab of Metastable Materials Science and Technology, Yanshan University, Qinhuangdao 066004, China.
Nano Letters
|September 22, 2025
Summary
Researchers developed a novel optical biosensing platform using surface plasmon resonance (SPR) and 2D GeP5 nanosheets for high-resolution protein analysis. This label-free method achieves single-amino acid resolution, advancing proteome studies.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Materials Science
Background:
- Accurate protein primary structure determination is crucial for understanding biological systems.
- Conventional peptide sequencing methods (Edman degradation, mass spectrometry) have limitations in sensitivity and sample input.
- Existing single-molecule sequencing methods face challenges due to limited labeling capabilities.
Purpose of the Study:
- To develop a versatile optical biosensing platform for high-resolution proteome analysis.
- To enhance sensitivity and real-time biomolecular interaction analysis.
- To enable label-free, single-amino acid resolution peptide sequencing.
Main Methods:
- Utilized surface plasmon resonance (SPR) technology for biosensing.
- Integrated 2D GeP5 nanosheets to enhance plasmonic response and SPR sensitivity.
- Developed a novel SPR system capable of recognizing and cleaving N-terminal amino acids sequentially.
Main Results:
- Achieved significant enhancement of the plasmonic response and SPR biosensor sensitivity.
- Demonstrated real-time scrutiny of biomolecular interactions.
- Attained single-residue resolution in peptide sequencing via a label-free "recognition-cleavage-re-recognition" process.
Conclusions:
- The developed SPR biosensing platform offers a sensitive and high-resolution method for proteome analysis.
- The integration of 2D GeP5 nanosheets significantly improves biosensor performance.
- This label-free approach overcomes limitations of existing sequencing techniques, particularly for low-abundance proteins.

