Identification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe.

ABSTRACT: Plasmodium falciparum causes the deadliest form of malaria. Adequate redox control is crucial for this protozoan parasite to overcome oxidative and nitrosative challenges, thus enabling its survival. Sulfenylation is an oxidative post-translational modification, which acts as a molecular on/off switch, regulating protein activity. To obtain a better understanding of which proteins are redox regulated in malaria parasites, we established an optimized affinity capture protocol coupled with mass spectrometry analysis for identification of in vivo sulfenylated proteins. The non-dimedone based probe BCN-Bio1 shows reaction rates over 100-times that of commonly used dimedone-based probes, allowing for a rapid trapping of sulfenylated proteins. Mass spectrometry analysis of BCN-Bio1 labeled prote

SUBMITTER: Schipper S 

PROVIDER: S-EPMC8218313 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature