1947-39-3

Upstream product

• 5241-58-7 L-Phenylalanine amide 
• 1152-61-0 N-Cbz-L-Asp 
• 5549-49-5 Z-Asp(OBu^t)-Phe-NH₂ 
• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 

Downstream Products

• 17327-68-3 N-Benzyloxycarbonyl-β-O-(2-dimethylamino-aethyl)-Asp-Phe-amid 
• 5241-71-4 Asp-Phe-NH₂ 
• 73537-63-0 Z-Asu-Phe-NH₂ 
• 138432-11-8 Asp-Phe*HBr 
• 17327-69-4 N-Benzyloxycarbonyl-β-O-(2-trimethylamonio-aethyl)-Asp-Phe-amid-jodid 
• 17471-91-9 β-O-2-Trimethylammonio-aethyl-Asp-Phe-amid-jodid 
• 63229-05-0 L-Methionyl-L-aspartyl-L-phenylalanine amide trifluoroacetate 
• 130832-06-3 Boc-Cle-Asp-Phe-NH₂ 
• 5920-14-9 N^α-tert-Butyloxycarbonyl-L-methionyl-L-aspartyl-L-phenylalanine amide 
• 138432-13-0 TFA*Neo-Asp-Phe-NH₂ 
• 138432-07-2 tert-butyloxycarbonylneopentylglycyl-aspartyl-phenylalanine amide 
• 114646-30-9 Boc-Leu-Asu-Phe-NH₂ 

Relevant academic research and scientific papers

Efficient chemo-enzymatic synthesis of endomorphin-1 using organic solvent stable proteases to green the synthesis of the peptide

Endomorphin-1 (Tyr-Pro-Trp-Phe-NH2, EM-1), an effective analgesic, was efficiently synthesized by a combination of enzymatic and chemical methods. Peptide Boc-Trp-Phe-NH2 was synthesized with a high yield of 97.1% by the solvent-stab

Aspartate Racemization in Synthetic Peptides. Part 2. Tendency to Racemization of Aminosuccinyl Residue

Aminosuccinyl (Asu) peptides, containing a strained ring system, are very vulnerable to epimerization and, during their formation, even as transients, in the presence of nucleophilic and nonnucleophilic bases, partial epimerization occurs.In the presence

SYNTHESIS OF THE CARBOXY-TERMINAL OCTAPEPTIDE OF CHOLECYSTOKININ (CCK-8) BASED ON INCORPORATION OF O4-SULFOTYROSINE BY ENZYMATICALLY CATALYZED FORMATION OF PEPTIDE BONDS

Papain-catalyzed condensation of sodium salt of tert-butyloxycarbonyl-β-tert-butyloxyaspartyl-O4-sulfotyrosine (fragment 1-2) with methionyl-glycyl-tryptophyl-methionyl-aspartyl-phenylalanine amide (fragment 3-8) has been elaborated.Deprotectio

ENZYMATIC SYNTHESIS OF ASPARTYL-CONTAINING DIPEPTIDES

We show that the ability of thermolysin to catalyze the coupling of aspartyl residue with other aminoacids is restricted to phenylalanine.Esterification of the two carboxylic groups of N-protected aspartic acid allows chymotrypsin and papain to catalyze the desired synthesis.