73994-88-4

Upstream product

• 4530-20-5 BOC-glycine 
• 73994-87-3 (S)-benzyl 2-((S)-2-amino-3-phenylpropanamido)-4-methylpentanoate hydrochloride 
• 74193-68-3 N-tert-butyloxycarbonyl-L-phenylalanyl-L-leucine benzyl ester 
• 1738-69-8 L-Leucine benzyl ester 
• 77066-56-9 benzyl-L-penylalanyl-L-leucinate trifluoroacetic acid 
• 3392-07-2 tert-butyl N-{2-[(2,5-dioxopyrrolidin-1-yl)oxy]-2-oxoethyl}carbamate 
• 1738-77-8 L-leucine benzyl ester p-toluenesulfonate 
• 3674-06-4 Boc-Phe-ONSu 
• 71027-08-2 (S)-4-Methyl-2-[(S)-2-(2-nitro-phenylsulfanylamino)-3-phenyl-propionylamino]-pentanoic acid benzyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 3655-05-8 tert-butoxycarbonylglycine p-nitrophenylester 
• 63649-15-0 L-phenylalanyl-L-leucine benzyl ester 
• 56406-63-4 N-(tert-butoxycarbonyl)glycine succinimide ester 

Downstream Products

• 73994-90-8 glycyl-L-phenylalanyl-L-leucine benzyl ester p-toluenesulfonate 
• 88159-10-8 Boc-Gly-Phe-Leu-Thr-OBn 
• 69729-14-2 benzyl ester of N-tert-butoxycarbonylglycylglycylphenylalanylleucine 
• 66328-74-3 Boc-Gly-Phe-Leu-OH 
• 77511-32-1 5>-enkephalin 
• 64963-27-5 N-tert-butyloxycarbonyl-L-tyrosyl-glycyl-glycyl-L-phenylalanyl-L-leucine 
• 63986-20-9 HCl·H-Tyr(OH)-Gly-Gly-Phe-Leu-OH 
• 948314-83-8 Leu⁵-Eukephalin 
• 69729-07-3 H-Gly-Gly-Phe-Leu-OBzl 
• 98695-49-9 Cbz-Tyr(Bzl)-β(BzlO)Ala-Gly-Phe-Leu-OBzl 
• 98695-47-7 Cbz-Tyr(Bzl)-(BzlO)Gly-Gly-Phe-Leu-OBzl 
• 98695-48-8 Cbz-Tyr(Bzl)-(BzlO)Ala-Gly-Phe-Leu-OBzl 
• 109022-57-3 H-(BzlO)Val-Gly-Phe-Leu-OBzl 
• 98695-45-5 H-(BzlO)Ala-Gly-Phe-Leu-OBzl 

Relevant academic research and scientific papers

Method of producing peptide

The present invention is related to a method of producing a peptide, characterized in contacting a reaction mixture with a base after a condensation reaction to hydrolyze while a basic condition is maintained until a ratio of a remaining unreacted active

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

Preparation and conformational study of CF3-containing enkephalin-derived oligopeptide

Incorporation of (2S,3S)-4,4,4-trifluorothreonine (F3-Thr) instead of Thr in the enkephalin-derived hexapeptide led to the apparent conformational alteration due to the strong electron-withdrawing effect of the trifluoromethyl group by comparison with the original compound on the basis of their various NMR measurements.

Introduction of F3-Threonine to the Hexapeptide, DSLET: Investigation of the Effect of Fluorine Atoms toward Peptidic Conformations

Introduction of trifluoromethyl-containing threonine to the target hexapeptide, Tyr-D-Ser-Gly-Phe-Leu-Thr (DSLET), led to the apparent conformational alteration due to the electron-withdrawing effect of the CF 3 group when compared with the ori

MW-enhanced high-speed deprotection of Boc group using p-TsOH and concommitant formation of N-Me-amino acid benzyl ester p-TsOH salts

A high-speed, complete deprotection of Boc group from Boc amino acids and protected peptide esters employing p-TsOH in toluene under microwave irradiation is found to be complete in 30s. The deprotection can be carried out in methanol and acetonitrile also. Under the present conditions, C-peptide benzyl esters and O-benzyl ethers have been found to be stable. This has permitted us to carry out the synthesis of [Leu]enkephalin employing the Boc/Bzl-group strategy. Further more, it has been found that both Nα-Fmoc and N α-Z groups are completely stable. The present conditions can be extended for the concomitant removal of the Boc group and the formation of C-benzyl amino acid esters as well. This has been utilized for the synthesis of N-Me amino acid benzyl esters starting from Boc-N-Me amino acids in a single step. Copyright Taylor & Francis, Inc.

N-Hydroxy Amides. Part 5. Synthesis and Properties of N-Hydroxypeptides having Leucine Enkephalin Sequences

In order to study the effects of the N-hydroxy amide group, N-hydroxyenkephalin analogues with the H-Tyr-(OH)X-Gly-Phe-Leu-OH sequence, where X=Gly, L-Ala, or β-Ala, have been synthesized.A (1)H n.m.r. study indicates that the N-hydroxyenkephalins have a type I β-turn structure in dimethyl sulphoxide solution.From the interaction of (HO)Gly- and β-(HO)Ala-analogues with Cu(II) it is suggested that the hydroxyamide function exerts a definite influence on the complexation.These N-hydroxyenkephalins are resistant to aminopeptidase M.A qualitative analgesia test shows that the (HO)Ala-analogue possesses a more lasting potency than that of Leu5-enkephalin, while having a comparable activity.

N-Hydroxy Amides. III. Active Esters of Polystyrene-bound 1-Hydroxy-2-pyrrolidinone and Their Use in Peptide Synthesis

A polymer-bond cyclic N-hydroxy amide has been prepared by reaction of aminomethylated copoly(styrene-2percent divinylbenzene) with 1-hydroxy-5-oxo-3-pyrrolidinecarboxylic acid using dicyclohexylcarbodiimide (DCC) as a condensing agent.Several N-blocked α-amino acids have been loaded on this resin by use of DCC.The amino acid resin can be utilized for peptide synthesis.Repetitive usage of the resin in the form of esters and facile synthesis of a biologically active pentapeptide, Leu5-enkephalin, show the usefulness of the polymer-bound 1-hydroxy-2-pyrrolidinone.

Studies on Amino Acids and Peptides. Part 6. Methods for Introducing Thioamide Bonds into the Peptide Backbone: Synthesis of the Four Monothio Analogues of Leucine Enkephalin

A methodology for preparing peptide analogues in which a thioamide bond replaces the normal amide bond is described.Thus, the synthesis of the three leucine enkephalin analogues 4>-, 2>-, and 1>-leucine enke