143294-03-5

Basic information

• Product Name: H-Tyr-D-Ala-Phe-Glu(<*>)-Val-Val-Lys(<*>)-NH₂
• CAS NO: 143294-03-5
• Molecular Weight: 836.001
• Mol File: 143294-03-5.mol

Chemical Properties

• CAS DataBase Reference: H-Tyr-D-Ala-Phe-Glu(<*>)-Val-Val-Lys(<*>)-NH₂(CAS DataBase Reference)
• NIST Chemistry Reference: H-Tyr-D-Ala-Phe-Glu(<*>)-Val-Val-Lys(<*>)-NH₂(143294-03-5)
• EPA Substance Registry System: H-Tyr-D-Ala-Phe-Glu(<*>)-Val-Val-Lys(<*>)-NH₂(143294-03-5)

Safety Data

• Hazardous Substances Data: 143294-03-5(Hazardous Substances Data)

Upstream product

• 3744-87-4 Boc-(R)-Ala 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2419-94-5 Boc-Glu 
• 20866-48-2 (S)-2-(tert-butoxycarbonylamino)-3-(4-(tert-butoxycarbonyloxy)phenyl)propanoic acid 
• 172542-14-2 Fmoc-Glu(OpNB)-OH 
• 68858-20-8 Fmoc-Val-OH 
• 35661-38-2 N-(9-fluorenylmethoxycarbonyl)-D-alanine 
• 174653-61-3 N_α-(9-fluorenylmethoxycarbonyl)-N_ε-(2-nitrobenzyloxycarbonyl)-lysine 

Relevant articles and documents

Semipermanent p-nitrobenzyloxycarbonyl (pNZ) protection of Orn and Lys side chains: Prevention of undesired α-Fmoc removal and application to the synthesis of cyclic peptides

Semipermanent side-chain protection of Orn and Lys with p-nitrobenzyloxycarbonyl (pNZ) for Fmoc/tBu chemistry does not result in the unwanted removal of α-Fmoc that occurs when groups such as Alloc are used for the same application. Furthermore, pNZ can be used in conjuction with p-nitrobenzyl ester (pNB) to prepare cyclic peptides.

Conformationally Restricted Deltorphin Analogues

Conformationally restricted deltorphin analogues were synthesized either through incorporation of cyclic phenylalanine analogues in position 2 or 3 of the peptide sequence or through various side chain-to-side chain cyclizations.Compounds were tested in μ-, δ-, and κ-receptor selective binding assays and in the guinea pig ileum (GPI) and mouse vas deferens (MVD) bioassays.Replacement of Phe3 in 2>deltorphin I with 2-aminoindan-2-carboxylic acid (Aic) or L- or D-2-aminotetralin-2-carboxylic acid (Atc) resulted in agonist compounds which retained the high δ receptor selectivity of the parent peptide.Substitution of a tetrahydroisoquinoline-3-carboxylic acid (Tic) residue in the 2-position of 2>deltorphin I and 4,Nle6>deltorphin produced a partial δ agonist, H-Tyr-Tic-Phe-Asp-Val-Val-Gly-NH2, and a pure δ antagonist, H-Tyr-Tic-Phe-Phe-Leu-Nle-Asp-NH2, respectively.The later antagonist displayed high δ selectivity (Kiμ/Kiδ=502) and was a potent antagonist against selective δ agonists in the MVD assay (Ke ca. 10 nM).Various 2>-deltorphin I analogues cyclized between the side chains of Orn (or Lys) and Asp (or Glu) residues substituted in positions 2 and 4, 4 and 7, and 2 and 7 were essentially nonselective.Comparison with corresponding N-terminal tetrapeptide analogues revealed that the C-terminal tripeptide segment in the deltorphin heptapeptides made a crucial contribution to δ affinity and δ selectivity in the case of the agonist peptides but not in the case of the antagonist.