79225-08-4

Upstream product

• 66959-85-1 Boc-Tyr(Bzl)-D-Ala-Gly-OBzl 
• 78537-07-2 N-(tert-butyloxycarbonyl)-L-tyrosyl-D-alanylglycine methyl ester 
• 64505-26-6 ethyl D-alanylglycinate 
• 2503-32-4 Z-D-Ala-Gly-OEt 
• 39897-54-6 D-Ala-Gly-OEt*HBr 
• 3978-80-1 Boc-Tyr-OH 
• 77621-73-9 Boc-Tyr-D-Ala-Gly-OEt 
• 71591-34-9 N-(tert-butyloxycarbonyl)-L-tyrosyl-D-alanine 
• 56-40-6 glycine 
• 1393358-73-0 C₂₂H₃₁N₃O₇ 
• 1393358-72-9 C₈H₁₄N₂O₃ 
• 74825-83-5 Boc-(L)(α-Me)Tyr-OH 
• 64410-45-3 D-Ala-Gly-OBzl*HCl 
• 67706-13-2 Boc-D-alanine-glycine-OMe 

Downstream Products

• 74814-33-8 Boc-Tyr(OH)-D-Ala-Gly-(aminomethyl)cyclobutane 
• 74814-28-1 Boc-Tyr(OH)-D-Ala-Gly-1-aminoindan 
• 107807-37-4 Boc-Tyr-D-Ala-Gly-(pN₃)Phe-Leu-OEt 
• 112157-37-6 C₆₈H₉₆N₁₀O₁₄S₂ 
• 112436-05-2 (Boc-Tyr-D-Ala-Gly-Phe-Leu-NH)2CHCH₂COOBzl 
• 75158-14-4 t-butoxycarbonyl-L-tyrosyl-D-alanyl-glycyl-L-phenylalanyl-L-t-butylglycine amide 
• 80972-73-2 Boc-Tyr-ala-Gly-Ada-Leu-NH₂ 
• 80768-22-5 Boc-Tyr-ala-Gly-Nip-Ada-NH₂ 
• 113845-51-5 N-Boc-L-tyrosyl-D-alanyl-glycl-L-β-(adeninyl-N⁹)-α-alanine methyl ester 
• 113845-43-5 N-Boc-L-tyrosyl-D-alanyl-glycl-L-β-(adeninyl-N⁹)-α-alanyl-L-leucine methyl ester 
• 113845-46-8 N-Boc-L-tyrosyl-D-alanyl-glycl-L-β-(adeninyl-N⁹)-α-alanyl-L-leucine amide 
• 135662-19-0 [(S)-1-[(R)-1-({[(S)-1-(2-Hydroxy-ethylcarbamoyl)-2-phenyl-ethylcarbamoyl]-methyl}-carbamoyl)-ethylcarbamoyl]-2-(4-hydroxy-phenyl)-ethyl]-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

Hydrazone linker as a useful tool for preparing chimeric peptide/ Nonpeptide bifunctional compounds

The area of multitarget compounds, joining two pharmacophores within one molecule, is a vivid field of research in medicinal chemistry. Not only pharmacophoric elements are essential for the design and activity of such compounds, but the type and length o

Factors that restrict the cell permeation of cyclic prodrugs of an opioid peptide, part 3: Synthesis of analogs designed to have improved stability to oxidative metabolism

Previously, our laboratory reported that cyclic peptide prodrugs of the opioid peptide H-Tyr-d-Ala-Gly-Phe-d-Leu-OH (DADLE) are metabolized by cytochrome P450 (CYP450) enzymes, which limits their systemic exposure after oral dosing to animals. In an attempt to design more metabolically stable cyclic prodrugs of DADLE, we synthesized analogs of DADLE cyclized with a coumarinic acid linker (CA; CA-DADLE), which contained modifications in the amino acid residues known to be susceptible to CYP450 oxidation. Metabolic stability and metabolite identification studies of CA-DADLE and its analogs were then compared using rat liver microsomes (RLM), guinea pig liver microsomes (GPLM), and human liver microsomes (HLM), as well as recombinant human recombinant cytochrome P450 3A4 (hCYP3A4). Similar to the results observed for CA-DADLE, incubation of its analogs with RLM, GPLM, and HLM resulted in monohydroxylation of an amino acid side chain on these cyclic prodrugs. When CA-DADLE was incubated with hCYP3A4, similar oxidative metabolism of the peptide was observed. In contrast, incubation of the CA-DADLE analogs with hCYP3A4 showed that these amino-acid-modified analogs are not substrates for this CYP450 isozyme. These results suggest that the amino-acid-modified analogs of CA-DADLE prepared in this study could be stable to metabolic oxidation by CYP3A4 expressed in human intestinal mucosal cells.

Synthesis and biological evaluation of new biphalin analogues with non-hydrazine linkers

Biphalin is a potent opioid peptide agonist, with a palandromic structure, composed of two enkephalin-like active fragments connected tail to tail by a hydrazine linker (Tyr-D-Ala-Gly-Phe-NH-NH-Phe-Gly-D-Ala-Tyr). This study presents the synthesis and

Amino acids and peptides. XXIV. Preparation and antinociceptive effect of [D-Ala2, (N-Me)Phe4]enkephalin analog-poly(ethylene glycol) hybrids

Hybrids of amino-poly(ethylene glycol) (aPEG) and [D-Ala2,(N-Me)Phe4]enkephalin analogs, H-Tyr-D-Ala-Gly-(Me)Phe-aPEG, H-Tyr-D-Ala-Gly-(Me)Phe-Leu-aPEG and H-Tyr-D-Ala-Gly-(Me)Phe-D-Leu-aPEG, were prepared by the solution method and

Investigation of the structural parameters involved in the μ and δ opioid receptor discrimination of linear enkephalin-related peptides

The previous rules proposed for selective recognition of μ and δ opioid receptors by modified enkephalins were investigated through an extensive structure-activity study. Thus, modifications of the sequence of TRIMU 4 (Tyr-D-Ala-Gly-NHCH(CH3)CH

Design and Synthesis of Enkephalin Analogues: Part II - Synthesis of 2, Met5>-Enkephalin Alkylamides Having Morphinomimetic Activity

Alkylamides of 2, Met5>-enkephalin have been synthesized by two different routes.The first method consists of the sequential peptidation of Phe-Met-ONBzl by 2,4,5-trichlorophenyl esters of Boc-Gly, Boc-D-Ala and Boc-Tyr to get

N-Adamantane-substituted tetrapeptide amides

N-Adamantane-substituted tetrapeptide amides and the pharmacologically acceptable salts thereof are disclosed herein. These compounds are analogs of enkephalin wherein the methionine or leucine of position 5 has been substituted by an adamantyl amide and the glycine of position 2 has been substituted by various amino acid residues. Optionally the tyrosine of position 1 and the phenylalanine of position 4 may be substituted by various amino acid residues. These compounds exhibit agonist activity at opiate receptor sites and are useful as analgesics.

Novel Analogues of Enkephalin: Identification of Functional Groups Required for Biological Activity

Novel tri- and tetrapeptide analogues of enkephalin, in conjunction with earlier structure-activity data, confirm that chemical substituents present in the first and fourth residues of enkephalin are required for in vitro biological activity.A class of ar