278185-22-1

Upstream product

• 75-31-0 isopropylamine 
• 14825-82-2 L-phenylalanine-N-carboxyanhydride 
• 16480-57-2 L-phenylalanine sodium salt 
• 84890-98-2 Fmoc-Phe-O-COO-isoBu 
• 35661-40-6 N-Fmoc L-Phe 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 78684-05-6 N-Benzyloxycarbonyl-(L)-Phenylalanine Isopropylamide 
• 143546-63-8 Boc-Phe-NHiPr 

Downstream Products

• 1552285-39-8 PhC(O)-Ala-4PiMS-Phe-NHiPr 
• 1552285-37-6 PhC(O)-Ala-3AzeS-Phe-NHiPr 
• 1552285-46-7 Boc-Ala-4PiMS-Phe-NHiPr 
• 1552285-45-6 Boc-Ala-3AzeS-Phe-NHiPr 
• 1552285-36-5 PhC(O)-4PiMS-Phe-NHiPr 
• 1552285-35-4 PhC(O)-3AzeS-Phe-NHiPr 
• 1552285-44-5 H-4PiMS-Phe-NHiPr 
• 1552285-43-4 H-3AzeS-Phe-NHiPr 
• 1552285-42-3 Cbz-4PiMS-Phe-NHiPr 
• 1552285-41-2 Cbz-3AzeS-Phe-NHiPr 
• 1420598-89-5 N-((((2S)-1-benzyloxycarbonylpyrrolidin-2-yl)methyl)sulfonyl)-L-phenylalanine isopropylamide 

Relevant academic research and scientific papers

C9/12 Ribbon-Like Structures in Hybrid Peptides Alternating α- and Thiazole-Based γ-Amino Acids

According to their restricted conformational freedom, heterocyclic γ-amino acids are usually considered to be related to Z-vinylogous γ-amino acids. In this context, oligomers alternating α-amino acids and thiazole-based γ-amino acids (ATCs) were expected to fold into a canonical 12-helical shape as described for α/γ-hybrid peptides composed of cis-α/β-unsaturated γ-amino acids. However, through a combination of X-ray crystallography, NMR spectroscopy, FTIR experiments, and DFT calculations, it was determined that the folding behavior of ATC-containing hybrid peptides is much more complex. The homochiral α/(S)-ATC sequences were unable to adopt a stable conformation, whereas the heterochiral α/(R)-ATC peptides displayed novel ribbon structures stabilized by unusual C9/12-bifurcated hydrogen bonds. These ribbon structures could be considered as a succession of pre-organized γ/α dipeptides and may provide the basis for designing original α-helix mimics.

METHOD OF SYNTHESIZING N-CARBOXYANHYDRIDE USING FLOW REACTOR

PROBLEM TO BE SOLVED: To provide a synthesis method that allows high-yield continuous production of a compound of interest in synthesis and production of N-carboxyanhydride (NCA) and the like using a flow reactor. SOLUTION: In a synthesis method using a flow reactor 100, a basic solution adjusted in advance to a pH of 7-14 becomes acidic with a pH of 0-7, or an acidic solution adjusted in advance to a pH of 0-7 becomes basic with a pH of 7-14, within 60 seconds after the start of mixture of at least two ingredient solutions. SELECTED DRAWING: Figure 1 COPYRIGHT: (C)2020,JPOandINPIT

Rapid and Mild Synthesis of Amino Acid N-Carboxy Anhydrides: Basic-to-Acidic Flash Switching in a Microflow Reactor

Polymerization of N-carboxy anhydrides (NCAs) is the primary process used to prepare polypeptides. The synthesis of various pure NCAs is key to the efficient synthesis of polypeptides. The only practical method that can be used to synthesize NCAs requires harsh acidic conditions that make acid-labile substrates unusable and results in an undesired ring opening of NCAs. Basic-to-acidic flash switching and subsequent flash dilution technology in a microflow reactor was used to demonstrate the synthesis of NCAs. It is both rapid (0.1 s) and mild (20 °C) and includes substrates containing acid-labile functional groups. The basic-to-acidic flash switching enabled both an acceleration of the desired NCA formation and avoided the undesired ring opening of NCAs. The flash dilution precluded the undesired decomposition of acid-labile functional groups. The developed process allowed the synthesis of various NCAs which cannot be readily synthesized using conventional batch methods.

Preparation of hydantoins by catalytic oxidative carbonylation of α-amino amides

(Chemical Equation Presented) Hydantoins can be synthesized from the corresponding amino amides employing oxidative catalytic carbonylation using W(CO)6 as the catalyst, I2 as the oxidant,COas the carbonyl source, andDBUas base. Secondary amides afford the hydantoins in good to excellent yields, which decrease as the steric bulk of the N-alkyl substituent increases. 2009 American Chemical Society.

Biological activity of cholecystokinin (30-33) tetrapeptide analogues

Analogues of the endogenous peptide corresponding to the 30-33 sequence of cholecystokinin (Trp-Met-Asp-Phe-NH2) were synthesized, and their biological activity was studied. It was shown that, in rats, the N-succinylated Nle2 analogu

Synthesis of amides from unprotected amino acids by a simultaneous protection-activation strategy using dichlorodialkyl silanes

Reaction of L-phenylalanine (1) with dichlorodimethylsilane or other dichlorosilane derivatives 6b-d and primary amines leads to the formation of amides probably via a cyclic silyl intermediate. It is also possible to use β-amino acids and N-alkylated amino acids (peptoid building blocks) as well as the amino dicarboxylic acid L-aspartic acid. The latter leads to almost exclusive formation of the α-amide.

Cyclopropane amino acids that mimic two χ1-conformations of phenylalanine

A highly constrained analogue of phenylalanine was prepared in optically pure form. This disubstituted cyclopropane amino acid, DiFi, realises two χ1 values of the phenylalanine side chain. Unlike monosubstituted analogues, amino acids of this