26061-29-0

Upstream product

• 13211-31-9 tert-butyl L-valinate 
• 1148-11-4 N-Benzyloxycarbonyl-L-proline 

Downstream Products

• 1432576-76-5 (S)-benzyl 2-((S)-1-((S)-1-tert-butoxy-1-oxopropan-2-ylamino)-3-methyl-1-oxobutan-2-ylcarbamoyl)pyrrolidine-1-carboxylate 
• 1432576-77-6 (S)-benzyl 2-((S)-1-((S)-1-tert-butoxy-3-methyl-1-oxobutan-2-ylamino)-3-methyl-1-oxobutan-2-ylcarbamoyl)pyrrolidine-1-carboxylate 
• 100690-01-5 Z-L-Pro-L-Val-L-Phe-Cm(O-t-Bu)-L-Val-OEt 
• 100689-92-7 Z-L-Phe-Cm(-L-Pro-L-Val-O-t-Bu)-L-Val-OEt 
• 100689-89-2 (S)-2-(Benzyloxycarbonyl-{2-[(S)-2-((S)-1-tert-butoxycarbonyl-2-methyl-propylcarbamoyl)-pyrrolidin-1-yl]-2-oxo-ethyl}-amino)-3-methyl-butyric acid ethyl ester 
• 21285-27-8 (2S)-2-[({(2S)-1-[(benzyloxy)carbonyl]tetrahydro-1H-pyrrol-2-yl}carbonyl)amino]-3-methylbutanoic acid 

Relevant academic research and scientific papers

Peptidomimetics for Targeting Protein-Protein Interactions between DOT1L and MLL Oncofusion Proteins AF9 and ENL

MLL-fusion proteins, AF9 and ENL, play an essential role in the recruitment of DOT1L and the H3K79 hypermethylation of MLL target genes, which is pivotal for leukemogenesis. Blocking these interactions may represent a novel therapeutic approach for MLL-rearranged leukemia. Based on the 7 mer DOT1L peptide, a class of peptidomimetics was designed. Compound 21 with modified middle residues, achieved significantly improved binding affinities to AF9 and ENL, with KD values of 15 nM and 57 nM, respectively. Importantly, 21 recognizes and binds to the cellular AF9 protein and effectively inhibits the AF9-DOT1L interactions in cells. Modifications of the N- and C-termini of 21 resulted in 28 with 2-fold improved binding affinity to AF9 and much decreased peptidic characteristics. Our study provides a proof-of-concept for development of nonpeptidic compounds to inhibit DOT1L activity by targeting its recruitment and the interactions between DOT1L and MLL-oncofusion proteins AF9 and ENL.

Amide formation in one pot from carboxylic acids and amines via carboxyl and sulfinyl mixed anhydrides

An efficient method has been developed for the preparation of yet unknown acyclic mixed anhydrides of carboxylic and sulfinic acids. Sterically hindered 2-methylbut-3-ene-2-sulfinyl carboxylates add primary and secondary amines preferentially onto the carbonyl moieties realizing a new method for the one-pot preparation of carboxamides. It uses 1:1 mixtures of carboxylic acids and amines without a base, requires no excess of reagents, and liberates only volatile coproducts. Protected di- and tripeptides have been prepared in solution without epimerization by application of this method.

Studies of Unusual Amino Acids and Their Peptides. XVII. The Synthesis of Peptides Containing N-Carboxymethyl Amino Acids. II.

The synthetic routes were investigated to four kinds of tetrapeptides made up of three usual amino acid residues and one N-carboxymethyl (Cm-) amino acid residue.The application of vacuum distillation made the isolation of a Cm-amino acid diester more convenient and efficient compared with the chromatographic methods which had been used previously.The efficiency of peptide bond formation at the imino group of a Cm-amino acid by the acid chloride method was remarkably improved under suitable reaction conditions.In the elongation of the peptide chain from a peptide containing a Cm-amino acid at the C-terminal position, the coupling efficiency was usually poorer than that in the case of the corresponding peptide composed only of the usual amino acid residues, and it depended greatly on the coupling methods, the 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide-1-hydroxybenzotriazole method being generaly the most desirable.

Cyclic esters of 3,4-dihydroxy-thiophene-1,1-dioxide compounds and 3,4-dihydroxy-cyclopentadienone compounds

Cyclic esters of 3,4-dihydroxy-thiophene-1,1-dioxide and of the corresponding cyclopentadienone compound, and their manufacture. The compounds can be used as "solid forms" of phosgene, thiophosgene or oxalyl chloride, or as acyl transfer agents.