A site-specific bioconjugation was developed based on direct aldol coupling using amino-acid-derived organocatalysts. The functionalization exhibits fast kinetics and occurs under mild, biocompatible conditions (viz., aqueous media, moderate temperature, and neutral pH). The resulting bioconjugates were found to be stable toward abundant aldolase enzymes, as well as acidic and basic pH. The methodology was demonstrated through conjugation of a variety of small molecules, dyes, and peptides to proteins, including a single-domain antibody, which was then used for cellular imaging.

Nitroalkanes react specifically with aldehydes, providing rapid, stable, and chemoselective protein bioconjugation. These nitroalkylated proteins mimic key post‐translational modifications (PTMs) of proteins and can be used to understand the role of these PTMs in cellular processes. Demonstrated here is the substrate scope of this bioconjugation by attaching a variety of tags, such as NMR tags, fluorescent tags, affinity tags, and alkyne tags, to proteins. The structure and enzymatic activity of modified proteins remain conserved after labeling. Notably, the nitroalkane group leads to easy characterization of proteins by mass spectrometry because of its distinct fingerprint pattern. Importantly, the nitro‐alkylated peptides provide a new handle for site‐selective fluorination of peptides, thus installing a specific probe to study peptide–protein interactions by 19F NMR spectroscopy. Furthermore, nitroalkane reagents can be used for the late‐stage diversification of peptides and for the synthesis of peptide staples.

Cetylpyridinium trichlorostannate (CPC-Sn), comprising cetylpyridinium chloride (CPC) and stannous chloride, was synthesized and characterized via single-crystal X-ray diffraction measurements indicating stoichiometry of C 21 H 38 NSnCl 3 where the molecules are arranged in a 1:1 ratio with a cetylpyridinium cation and a [SnCl 3 ] − anion. CPC-Sn has shown potential for application as a broad-spectrum antimicrobial agent, to reduce bacteria-generated volatile sulfur compounds and to produce advanced functional materials. In order to investigate its controlled-release properties, electrical resistance tomography was implemented. The results demonstrate that CPC-Sn exhibits extended-release properties in an aqueous environment as opposed to the CPC counterpart.

Nitroalkanes react specifically with aldehydes, providing rapid, stable, and chemoselective protein bioconjugation. These nitroalkylated proteins mimic key post‐translational modifications (PTMs) of proteins and can be used to understand the role of these PTMs in cellular processes. Demonstrated here is the substrate scope of this bioconjugation by attaching a variety of tags, such as NMR tags, fluorescent tags, affinity tags, and alkyne tags, to proteins. The structure and enzymatic activity of modified proteins remain conserved after labeling. Notably, the nitroalkane group leads to easy characterization of proteins by mass spectrometry because of its distinct fingerprint pattern. Importantly, the nitro‐alkylated peptides provide a new handle for site‐selective fluorination of peptides, thus installing a specific probe to study peptide–protein interactions by 19F NMR spectroscopy. Furthermore, nitroalkane reagents can be used for the late‐stage diversification of peptides and for the synthesis of peptide staples.