138228-90-7

Upstream product

• 5473-12-1 N-methylglycine methylester 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 501-53-1 benzyl chloroformate 
• 63-91-2 L-phenylalanine 
• 1161-13-3 N-Cbz-L-Phe 
• 13515-93-0 N-methylglycine methyl ester hydrochloride 

Downstream Products

• 138229-12-6 diphenyl 2.1-<(benzyloxy)carbonyl>-L-phenylalanyl-(2,2-decarboxy-N^2.2-methyl-L-phenylalanin-2,2-yl)>phosphonate 
• 138229-12-6 diphenyl 2.1-<(benzyloxy)carbonyl>-L-phenylalanyl-(2,2-decarboxy-N^2.2-methyl-D-phenylalanin-2,2-yl)>phosphonate 
• 138229-06-8 diphenyl 2.1-<(benzyloxy)carbonyl>-L-phenylalanyl-(2,2-decarboxy-N^2.2-methyl-3,2-vinyl-L-alanin-2,2-yl)>phosphonate 
• 138229-06-8 diphenyl 2.1-<(benzyloxy)carbonyl>-L-phenylalanyl-(2,2-decarboxy-N^2.2-methyl-3,2-vinyl-D-alanin-2,2-yl)>phosphonate 
• 138228-96-3 diphenyl N^2.1-<(benzyloxy)carbonyl>-L-phenylalanyl-(2,2-decarboxysarcosin-2,2-yl)phosphonate 
• 138228-93-0 N²-<(benzyloxy)carbonyl>-N¹-(methoxymethyl)-N¹-methyl-L-phenylalaninamide 
• 99997-51-0 N^2.1-<(benzyloxy)carbonyl>-L-phenylalanylsarcosine 

Relevant academic research and scientific papers

Practical Peptide Synthesis Mediated by a Recyclable Hypervalent Iodine Reagent and Tris(4-methoxyphenyl)phosphine

6-(3,5-Bis(trifluoromethyl)phenyl)-1H,4H-2aλ3-ioda-2,3-dioxacyclopenta[hi]indene-1,4-dione (p-BTFP-iodosodilactone, 1a) was synthesized and demonstrated to be an efficient hypervalent iodine(III) reagent for the synthesis of dipeptides from various standard amino acids, including sterically hindered amino acids, in good to high yields within 30 min in the presence of tris(4-methoxyphenyl)phosphine. In addition, the combined system of 1a/(4-MeOC6H4)3P was used to synthesize the pentapeptide leu-enkephalin in protected form. It is worth noting that 1a can be regenerated readily after reaction.

Efficient peptide coupling involving sterically hindered amino acids

(Chemical Equation Presented) Hindered amino acids have been introduced into peptide chains by coupling N-(Cbz- and Fmoc-α-aminoacyl) benzotriazoles with amino acids, wherein at least one of the components was sterically hindered, to provide compounds 3a-e, (3c +3 c′), 5a-d, (5a + 5a′), 6a-c, (6b + 6b′), 8a-c, 9a-e, 10a-d, and (10a + 10a′) in isolated yields of 41-95% with complete retention of chirality as evidenced by NMR and HPLC analysis. The benzotriazole activation methodology is a new route for the synthesis of sterically hindered peptides. (Note: compound numbers written within brackets represent diastereomeric mixtures or racemates; compound numbers without brackets represent enantiomers.)

Influence of solvent viscosity on the rate of hydrolysis of dipeptides by carboxypeptidase Y

The influence of solvent viscosity on the rate of enzymatic hydrolysis of a series of dipeptides (Z-Phe-Gly, Z-Phe-Sar, Z-Phe-Ala, Z-Phe-NMeAla, Z-Phe-Aib and Z-Phe-Pro) by carboxypeptidase Y was investigated. The effect of solvent viscosity on the enzymatic hydrolysis revealed that whereas all Kcat values decreased with viscosity, those of the N-alkyl peptides decreased more than those of the N-H peptides. The kinetic behaviour implies the involvement of conformational changes of the enzyme in terms of the 'induced-fit' process. Copyright