783350-39-0

Upstream product

• 323198-14-7 2-amino-pentanedioic acid 1-[(4-methyl-2-oxo-2H-chromen-7-yl)-amide] 5-trityl-amide 
• 4289-98-9 N-formyl-L-methionine 
• 132327-80-1 Fmoc-L-Gln(Trt)-OH 
• 26093-31-2 7-amino-4-methylcoumarin. 
• 422309-19-1 7-(N^α-9-fluorenylmethoxycarbonyl-N^γ-trityl-L-glutamyl)amino-4-methylcoumarin 

Relevant academic research and scientific papers

Slow-binding inhibition of peptide deformylase by cyclic peptidomimetics as revealed by a new spectrophotometric assay

A new spectrophotometric/fluorimetric assay for peptide deformylase (PDF) has been developed by coupling the PDF reaction with that of dipeptidyl peptidase I (DPPI) and using N-formyl-Met-Lys-AMC as substrate. Removal of the N-terminal formyl group by PDF renders the dipeptide an efficient substrate of DPPI, which subsequently removes the dipeptidyl units to release 7-amino-4-methylcoumarin as the chromophore/fluorophore. The PDF reaction is conveniently monitored on a UV-Vis spectrophotometer or a fluorimeter in a continuous fashion. The utility of the assay was demonstrated by determining the catalytic activity of PDF and the inhibition constants of PDF inhibitors. These studies revealed the slow-binding behavior of a previously reported macrocyclic PDF inhibitor. This method offers several advantages over the existing PDF assays and should be particularly useful for screening PDF inhibitors in the continuous fashion.