63631-32-3

Upstream product

• 4530-20-5 BOC-glycine 
• 19240-24-5 N--L-3-phenylalanine methyl ester hydrochloride 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 203053-87-6 (S)-methyl 2-(2-aminoacetamido)-3-phenylpropanoate trifluoroacetate salt 
• 63-91-2 L-phenylalanine 
• 3392-07-2 tert-butyl N-{2-[(2,5-dioxopyrrolidin-1-yl)oxy]-2-oxoethyl}carbamate 
• 106624-70-8 methyl (2S)-2-[[2-(t-butoxycarbonylamino)acetyl]amino]-3-phenylpropanoate 
• 31972-52-8 Boc-Gly-Gly-OH 

Downstream Products

• 35671-84-2 N-acetyl-glycyl-glycyl-L-phenylalanine methyl ester 
• 14281-57-3 N-acetyl-glycyl-L-phenylalanine methyl ester 
• 3618-96-0 (S)-N-acetylphenylalanine 
• 80164-29-0 N-t-butoxycarbonylglycylglycyl-L-phenylalanyl-L-leucine methyl ester 
• 77511-32-1 5>-enkephalin 
• 61196-05-2 Boc-Tyr(Bzl)-Gly-Gly-Phe-OMe 
• 61131-30-4 Boc-L-Tyr(Bzl)-Gly-Gly-L-Phe-OH 
• 64963-27-5 N-tert-butyloxycarbonyl-L-tyrosyl-glycyl-glycyl-L-phenylalanyl-L-leucine 
• 75244-08-5 4-nitrobenzyl ester of N-benzyloxycarbonyl-O-benzyl-L-tyrosylglycylglycyl-L-phenylalanyl-L-leucine 
• 81649-51-6 hydrochloride of 4-nitrobenzyl ester of glycyl-glycyl-L-phenylalanyl-L-leucine 
• 75244-06-3 4-nitrobenzyl ester of N-t-butyloxycarbonylglycylglycyl-L-phenylalanyl-L-leucine 
• 501082-99-1 C₅₇H₆₈Cl₂N₆O₁₀ 
• 521060-85-5 C₅₅H₆₆Cl₂N₆O₉ 
• 501082-88-8 C₅₈H₇₁Cl₂N₅O₁₀ 

Relevant academic research and scientific papers

Phenysilane and Silicon Tetraacetate: Versatile Promotors for Amide Synthesis

Phenylsilane was reevaluated as a useful coupling reagent for amide synthesis. At room temperature, a wide range of amides and peptides were obtained in good to excellent yields (up to 99 %). For the first time, Weinreb amides synthesis mediated by a hydrosilane were also documented. Comparative experiments with various acetoxysilanes suggested the involvement of a phenyl-triacyloxysilane. From this mechanistic study, silicon tetraacetate was shown as an efficient amine acylating agent.

Pd-Catalyzed Site-Selective C(sp2)-H Olefination and Alkynylation of Phenylalanine Residues in Peptides

Pd-catalyzed site-selective C(sp2)-H olefination and alkynylation of phenylalanine residues in peptides are described. The amino acids within the peptides are used as native bidentate directing groups to facilitate C-H functionalization. This p

Diphenylsilane as a coupling reagent for amide bond formation

A simple procedure for amide bond formation using diphenylsilane as a coupling reagent is described. This methodology enables the direct coupling of carboxylic acids with primary and secondary amines, releasing only hydrogen and a siloxane as by-products. Only one equivalent of each partner is needed, providing a more sustainable amidation method producing minimal wastes. This methodology was also extended to the synthesis of peptides and lactams by addition of Hünig's base (DIPEA) and 4-dimethylaminopyridine (DMAP).

Fragmentation-Rearrangement of Peptide Backbones Mediated by the Air Pollutant NO2.

The fragmentation-rearrangement of peptide backbones mediated by nitrogen dioxide, NO2., was explored using di-, tri-, and tetrapeptides 8-18 as model systems. The reaction, which is initiated through nonradical N-nitrosation of the peptide bond, shortens the peptide chain by the expulsion of one amino acid moiety with simultaneous fusion of the remaining molecular termini through formation of a new peptide bond. The relative rate of the fragmentation-rearrangement depends on the nature of the amino acids and decreases with increasing steric bulk at the α carbon in the order Gly>Ala>Val. Peptides that possessed consecutive aromatic side chains only gave products that resulted from nitrosation of the sterically less congested N-terminal amide. Such backbone fragmentation-rearrangement occurs under physiologically relevant conditions and could be an important reaction pathway for peptides, in which sections without readily oxidizable side chains are exposed to the air pollutant NO2.. In addition to NO2.-induced radical oxidation processes, this outcome shows that ionic reaction pathways, in particular nitrosation, should be factored in when assessing NO2. reactivity in biological systems.

Environmentally benign peptide synthesis using liquid-assisted ball-milling: Application to the synthesis of Leu-enkephalin

This paper describes an original methodology for peptide bond synthesis avoiding toxic solvents and reactants. Ball-milling stoichiometric amounts of Boc-protected α-amino acid N-carboxyanhydrides (Boc-AA-NCA) or Boc-protected α-amino acid N-hydroxysuccin

FLUORINATION OF ORGANIC COMPOUNDS

Methods for fluorinating organic compounds are described herein.

Silver-catalyzed late-stage fluorination

Carbon-fluorine bond formation by transition metal catalysis is difficult, and only a few methods for the synthesis of aryl fluorides have been developed. All reported transition-metal-catalyzed fluorination reactions for the synthesis of functionalized arenes are based on palladium. Here we present silver catalysis for carbon-fluorine bond formation. Our report is the first example of the use of the transition metal silver to form carbon-heteroatom bonds by cross-coupling catalysis. The functional group tolerance and substrate scope presented here have not been demonstrated for any other fluorination reaction to date.

Studies on the synthesis and anti-Osteoporosis of estrogen-GHRPs linkers.

The linkers of estrogen-GHRPs were prepared by the combination of estradiol, estrone, TyrGlyGlyPheLeuOH, and TyrGlyGlyPheLeuOH. Their anti-osteoporosis effect was evaluated by analyzing the data, for instance the weight of the body, femur, femur ash, the content of calcium and phosphor in the femur, the content of calcium and ALP activity in the serum, obtained from the corresponding bioassay in vivo. The results indicated that the anti-osteoporosis potency for estradiol, estrone, TyrGlyGlyPheLeuOH and TyrGlyGlyPheLeuNH(2) may be totally enhanced each other via the corresponding linkers.

L-Selective dipeptide synthesis using novel thermophilic enzyme from Clostridium sp.

A novel, inexpensive, thermophilic protease-type enzyme isolated from Clostridium thermohydrosulfuricum was used for dipeptide synthesis. The enzyme showed broad substrate selectivity and enantioselectivity towards L-amino acids in peptide bond formation.

Additives Based on Liquid Crystal Forming Structure Elements for Suppressing Racemization in Peptide Synthesis by the DCC- and Mixed Anhydrides Methods

A new type of additives suppressing racemization during peptide synthesis by the DCC- and mixed anhydrides methods are liquid crystal forming organic molecules or similar compounds with a specific long chain structure.The suppressing effect of the new additives was followed by the Anderson test, the modifid Young and n.m.r. tests.There was no racemization in a new Leu-enkephalin synthesis by the mixed anhydrides method with azoxybenzene as additive.