19963-33-8

Upstream product

• 15761-38-3 L-N-Boc-Ala 
• 41036-19-5 L-alanyl-alanine methylester hydrochloride 

Downstream Products

• 88874-01-5 N^h-(L-alanyl-alanyl-alanyl) isonicotinic acid hydrazide dihydrochloride 
• 155518-27-7 N^α-tert-butoxycarbonyl-L-alanyl-L-alanyl-L-alanyl-(N^ε-benzyloxycarbonyl)-L-lysyl-L-alanyl-(N^ε-(benzo-18-crown-6)-4-carbonyl)-L-lysyl-L-alanine methyl ester 
• 41036-27-5 H-Ala₃-OMe*HCl 

Relevant academic research and scientific papers

Peptide-tethered monodentate and chelating histidylidene metal complexes: Synthesis and application in catalytic hydrosilylation

The Nδ,Nε-dimethylated histidinium salt (His*) was tethered to oligopeptides and metallated to form Ir(iii) and Rh(i) NHC complexes. Peptide-based histidylidene complexes containing only alanine, Ala-Ala-His*-[M] and Ala-Ala-Ala-His*-[M] were synthesised ([M] = Rh(cod)Cl, Ir(Cp*)Cl2), as well as oligopeptide complexes featuring a potentially chelating methionine and tyrosine residue, Met-Ala-Ala-His*-Rh(cod)Cl and Tyr-Ala-Ala-His*-Rh(cod)Cl. Chelation of the methionine-containing histidylidene ligand was induced by halide abstraction from the rhodium centre, while tyrosine remained non-coordinating under identical conditions. High catalytic activities in hydrosilylation were achieved with all peptide-based rhodium complexes. The cationic S Met,CHis*-bidentate peptide rhodium catalyst outperformed the monodentate neutral peptide complexes and constitutes one of the most efficient rhodium carbene catalysts for hydrosilylation, providing new opportunities for the use of peptides as N-heterocyclic carbene ligands in catalysis.

Intramolecular ligation of carbonyl oxygen to central zinc in synthetic oligopeptide-linked zinc-porphyrins

Oligopeptide-linked zinc-porphyrins were prepared (oligopeptide = -Phe(m)-Ala(n)-OMe and porphyrin = 5,15-diaryl-2,3,7,8,12,13,17,18-octaethylporphyrin). 1H NMR, IR, visible, and CD spectra of the synthetic molecule in a chlorinated methane (CDCl3 or CH2Cl2) showed that the carbonyl oxygen of the N-terminal amino acid of the linked peptide should ligate the central zine metal in the molecule as the axial ligand to form a pentacoordinated zinc-porphyrin. The coordination of the zinc with the peptide framework changed the optical and electrical properties, indicating that such ligation might control the reactivity in biological metallotetrapyrrole-protein systems as well as the coordination to the peptide residue.

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.