Fig. 1: The trifunctional reductant-cleavable chemical proteomic probe OPA-S-S-alkyne for fast labeling of lysine. | Nature Communications

Fig. 1: The trifunctional reductant-cleavable chemical proteomic probe OPA-S-S-alkyne for fast labeling of lysine.

From: A chemical proteomics approach for global mapping of functional lysines on cell surface of living cell

Fig. 1: The trifunctional reductant-cleavable chemical proteomic probe OPA-S-S-alkyne for fast labeling of lysine.

a The chemical structure of OPA-S-S-alkyne and chemical reaction between the probe and lysine on peptides or proteins in PBS buffer (pH = 7.4). b MALDI MS spectra of the model peptide (Ac-GGYTLVSGYPK) before (top) and after (bottom) reaction with OPA-S-S-alkyne. c Reaction rate assay of model peptide (Ac-GGYTLVSGYPK) with different equivalent OPA-S-S-alkyne over time (0.5 min, 1 min, 2 min, 3 min, 5 min, and 10 min). d MALDI MS spectra of myoglobin protein before (top) and after (bottom) modified with OPA-S-S-alkyne. The numbers marked in red represent how many lysines of myoglobin are modified by OPA-S-S-alkyne. e In-gel fluorescence scanning of the protein covalent labeled by OPA-S-S-alkyne followed by click with CalFluor 488 Azide. Top: Concentration-dependent labeling of BSA protein for 30 min; Bottom: Time-dependent labeling of BSA protein (10 µM). Images shown are representative of three independent experiments. Source data are provided as a Source Data file.

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