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Related Experiment Video

Updated: Jan 5, 2026

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

OPA-Based Bifunctional Linker for Protein Labeling and Profiling.

Qing Zhang¹, Yue Zhang¹, Heng Liu¹

¹Department of Chemistry, State Key Laboratory of Synthetic Chemistry , The University of Hong Kong , Hong Kong , People's Republic of China, SAR.

|October 29, 2019

Summary

This summary is machine-generated.

Researchers developed a new ortho-phthalaldehyde (OPA)-based linker for efficient protein labeling. This OPA-NH-alkyne linker offers a cost-effective and stable alternative for chemical modification and profiling of proteins.

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Area of Science:

Biochemistry
Chemical Biology
Proteomics

Background:

Lysine residues are common sites for protein chemical labeling and modification.
Existing lysine-labeling agents present challenges in efficiency, stability, and cost.

Purpose of the Study:

To develop novel bifunctional linkers for protein chemical labeling and profiling.
To identify an optimal ortho-phthalaldehyde (OPA)-based linker for improved protein modification.

Main Methods:

Design and synthesis of three OPA-based bifunctional linkers.
Evaluation of linker performance for protein labeling, focusing on efficiency and minimizing protein turbidity.
Demonstration of the optimal linker's applicability in immediate protein and proteome capture labeling.

Main Results:

OPA-NH-alkyne 5 was identified as the optimal OPA-based bifunctional linker.
This linker demonstrated efficient protein labeling with minimal induced protein turbidity.
The OPA-NH-alkyne 5 linker proved effective for immediate capture of proteins and proteomes.

Conclusions:

The developed OPA-NH-alkyne 5 linker provides an effective and potentially cost-efficient strategy for protein chemical labeling.
This new reagent expands the toolkit for protein modification, profiling, and proteomic studies.