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• 152754-55-7 (S)-methyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate 
• 220903-94-6 (S)-methyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate 
• 215168-76-6 (R)-N-(tert-butyloxycarbonyl)-1-(3-aminophenyl)-3-(3,4-dimethoxyphenyl)propan-1-ol 
• 215168-75-5 tert-butyl (3-(3-(3,4-dimethoxyphenyl)propanoyl)phenyl)carbamate 
• 18650-39-0 (S)-methyl pipecolinate hydrochloride 
• 215168-74-4 1-(3-aminophenyl)-3-(3,4-dimethoxyphenyl)-1-propanone 
• 75573-20-5 (2E)-3-(3,4-dimethoxyphenyl)-1-(3-nitrophenyl)-2-propen-1-one 
• 121-89-1 3-Nitroacetophenone 
• 124093-26-1 methyl (S)-1-(2-methoxy-2-oxoacetyl)piperidine-2-carboxylate 
• 120-14-9 3,4-dimethoxy-benzaldehyde 
• 153086-78-3 tert-butyl {2-[2-(2-aminoethoxy)ethoxy]ethyl}carbamate 
• 929-59-9 3,6-dioxa-1,8-diaminooctane 
• 195513-96-3 SLF 
• 215168-85-7 (1R)-1-[3-N-(tert-butyloxycarbonyl)aminophenyl]-3-(3,4-dimethoxyphenyl)-1-propanyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate 

Relevant academic research and scientific papers

Targeted Covalent Inhibition of Plasmodium FK506 Binding Protein 35

FK506-binding protein 35, FKBP35, has been implicated as an essential malarial enzyme. Rapamycin and FK506 exhibit antiplasmodium activity in cultured parasites. However, due to the highly conserved nature of the binding pockets of FKBPs and the immunosuppressive properties of these drugs, there is a need for compounds that selectively inhibit FKBP35 and lack the undesired side effects. In contrast to human FKBPs, FKBP35 contains a cysteine, C106, adjacent to the rapamycin binding pocket, providing an opportunity to develop targeted covalent inhibitors of Plasmodium FKBP35. Here, we synthesize inhibitors of FKBP35, show that they directly bind FKBP35 in a model cellular setting, selectively covalently modify C106, and exhibit antiplasmodium activity in blood-stage cultured parasites.

Fluorophore labeling of native FKBP12 by ligand-directed tosyl chemistry allows detection of its molecular interactions in vitro and in living cells

Introducing synthetic fluorophores into specific endogenous proteins and analyzing their function in living cells are a great challenge in chemical biology. Toward this end, we demonstrate the target-selective and site-specific fluorescent labeling of native FKBP12 (FK506-binding protein 12) in vitro and in living cells using ligand-directed tosyl (LDT) chemistry. The LDT-mediated labeling yielded a semisynthetic FKBP12 containing the Oregon green (OG) dye near the catalytic pocket. The OG-labeled FKBP12 (OG-FKBP12) acted as a fluorescent reporter that allows monitoring of its interaction with rapamycin and FRB (FKBP-rapamycin-binding domain) in vitro. We also successfully demonstrated the visualization of the rapamycin-mediated complexation of the OG-FKBP12 and FRB inside of living cells by the combined use with fluorescent protein-tag technology and Foerster resonance energy-transfer imaging.