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Bioinspired Nitroalkylation for Selective Protein Modification and Peptide Stapling.

Sriram Mahesh¹, Victor Adebomi¹, Zilma P Muneeswaran²

¹Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, 36830, USA.

Angewandte Chemie (International Ed. in English)

|November 28, 2019

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Nitroalkanes enable precise protein bioconjugation, creating modified proteins that mimic natural post-translational modifications (PTMs). This technique allows for diverse tagging and analysis, aiding in understanding protein function and interactions.

Area of Science:

Biochemistry
Chemical Biology
Proteomics

Background:

Post-translational modifications (PTMs) are crucial for protein function.
Understanding PTMs requires specific labeling and analysis techniques.

Purpose of the Study:

To introduce a novel nitroalkane-aldehyde reaction for chemoselective protein bioconjugation.
To demonstrate the utility of this method for mimicking PTMs and enabling diverse applications.

Main Methods:

Utilized nitroalkanes for specific reaction with aldehyde groups on proteins.
Attached various tags (NMR, fluorescent, affinity, alkyne) to proteins.
Analyzed modified proteins using mass spectrometry and ¹⁹F NMR spectroscopy.

Main Results:

Keywords:

amino acids chemoselectivity nitroalkylation peptides proteins

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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

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Achieved rapid, stable, and chemoselective protein labeling.
Maintained protein structure and enzymatic activity post-labeling.
Nitroalkane modification facilitated mass spectrometry characterization.
Enabled site-selective fluorination for peptide-protein interaction studies.

Conclusions:

Nitroalkane bioconjugation is a versatile tool for protein modification and PTM mimicry.
This method supports diverse applications in proteomics, chemical biology, and structural studies.
Offers new avenues for peptide diversification and synthesis.