88874-01-5

Usage

InChI:InChI=1/C15H22N6O4.2ClH/c1-8(16)12(22)18-9(2)13(23)19-10(3)14(24)20-21-15(25)11-4-6-17-7-5-11;;/h4-10H,16H2,1-3H3,(H,18,22)(H,19,23)(H,20,24)(H,21,25);2*1H/t8-,9-,10-;;/m0../s1

Upstream product

• 19963-33-8 N^α-tert-butoxycarbonyl-L-alanyl-L-alanyl-L-alanine methyl ester 
• 41036-19-5 L-alanyl-alanine methylester hydrochloride 
• 27317-70-0 N^α-tert-butoxycarbonyl-L-alanyl-L-alanyl-L-alanine 
• 54-85-3 isoniazid 
• 88874-00-4 N^h-(N-tert-butyloxycarbonyl-L-alanyl-alanyl-alanyl)-isonicotinic acid hydrazide 

Relevant academic research and scientific papers

Synthesis and biological activities of the tri-L-alanine derivative of isonicotinic acid hydrazide

N-(tert-Butyloxycarbonyl) tri-L-alanine was coupled to the hydrazide function of isonicotinic acid hydrazide followed by cleavage of the amino protective group. The resulting dihydrochloride of the tri-L-alanine derivative of isonicotinic acid hydrazide was characterized by 13C-NMR. The minimal inhibitory concentration of isonicotinic acid hydrazide was not improved by the peptide derivative, and competition experiments with tri-L-alanine demonstrated that tri-L-alanyl-isonicotinic acid hydrazide did not use the peptide transport system. Isonicotinic acid hydrazide and its tri-peptide derivative possessed the same activity against pathogenic mycobacteria and did not antagonize each other. The relatively high stability of the tri-peptide derivative against peptidases of Mycobacterium fortuitum was discussed as being responsible for the significantly weaker activity against this atypical mycobacterium strain. With the exception of peptidases of hog intestinal mucosa, the tri-L-alanyl derivative of isonicotinic acid hydrazide was stable against pronase and α-chymotrypsin when compared to other peptides.