60421-25-2

Upstream product

• 62-57-7 2-Aminoisobutyric acid 
• 2258-42-6 formyl acetic anhydride 
• 64-18-6 formic acid 

Downstream Products

• 99991-67-0 N-Formyl-2-methyl-alanin-cyclohexylamid 
• 1370651-96-9 C₃₄H₄₉N₇O₇S 
• 1370651-92-5 C₄₆H₅₇N₇O₇S 
• 1370651-86-7 C₃₀H₄₃N₅O₅S 
• 145645-78-9 trans-2-Formylamino-2-methyl-N-(4-nitroxycyclohexyl)-propionsaeureamid 
• 71015-20-8 2-carbomethoxy-2-methylethyl isocyanide 
• 133859-55-9 N-formyl-α-aminoisobutyric acid phenyl ester 

Relevant academic research and scientific papers

Thioester-isocyanides: Versatile reagents for the synthesis of cycle-tail peptides

A novel class of reagents, thioester isocyanides, have been prepared and applied in the synthesis of peptide macrocycles. The isocyanide part of the molecule is deployed in a multicomponent macrocyclization step. This step is followed by chemoselective peptide ligation at the thioester part of the macrocycle. Our method can now be used for rapid assembly and evaluation of cycle-tail peptides. The Royal Society of Chemistry 2012.

Remote binding energy in antibody catalysis: Studies of a catalytically unoptimized specificity pocket

Binding interactions remote from the hydrolytic reaction center have been probed with substrate and phosphonate transition state analogues to understand how these types of interactions are used to promote catalysis in the 17E8 system. We find that the hapten-generated recogniton pocket in 17E8 has properties that are analogous to those of specificity pockets in enzymes. We have also found that there are specific requirements to form catalytically productive interactions between the side chain and the recognition pocket including conformation, size, and geometry. An additional requirement includes favorable simultaneous interactions between the side chain and binding pocket along with favorable interactions with the oxyanion hole. The 17E8 side chain recognition pocket seems to be less catalytically efficient than analogous pockets in enzymatic systems. The apparent binding energy gained from the methylene-pocket interactions in the 17E8 system is significantly smaller than those observed in natural enzymes. Furthermore, 17E8 does not use specific interactions in the recognition pocket to significantly affect catalytic turnover (kcat) which is thought to be a trait of an unoptimized catalyst. Analysis of the crystal structure of the 17E8·hapten complex has allowed for the identification of differences between the active sites of 17E8 and several proteases. The identified differences give insight to the sources of the inefficient use of binding energy.

N-chloro-amino acid derivatives activity

There is provided, a novel class of compounds exhibiting antibacterial activity, said compounds having the formula: EQU1 wherein X and Y each represent a member which may be the same or different selected from the group consisting of H and Cl with the pri