We report the synthesis and biological profiling of photoreactive chemical probes based on an established plasmepsin X inhibitor scaffold. Maintained antimalarial and recombinant enzyme activity support their use in future chemical proteomic studies.
The clickable and photoreactive amino acid is prepared in 11 steps from 3-(4-bromophenyl)-1-propanol.
This study introduces new photoaffinity-based probes to identify mono-ADP-ribose readers. Using human cell extracts, it detects both known and potential readers, thereby improving our understanding of mono-ADP-ribosylation.
Antibiotic resistance is an enormous problem that is accountable for over a million deaths annually, with numbers expected to significantly increase. Chemical tools can help to uncover the molecular mechanisms involved in resistance development.
Chemoproteomic and genetic approaches reveal sterol interactions with stimulator of interferon genes (STING)-sterol, with subcellular localization and activation also responsive to sterol content.