58822-25-6Relevant articles and documents
Cobalt(III)-Mediated Peptide Synthesis. 2. Synthesis of Tetrapeptides and 5>enkephalin
Knighton, D. R.,Harding, D. R. K.,Friar, M. J.,Hancock, W. S.,Reynolds, G. D.,et al.
, p. 7025 - 7026 (1981)
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The pivaloylglycol anchor group: A new platform for a photolabile linker in solid-phase synthesis
Peukert, Stefan,Giese, Bernd
, p. 9045 - 9051 (1998)
We have designed a new photolabile linker (2) based on 2- pivaloylglycerol for the solid-phase synthesis of acids. The linker was prepared in six steps and anchored to the support via an amide bond. Photocleavage is a two-step process, in which the immobilized acids are released by photolyric generation of a radical center and subsequent spontaneous β-C,O bond scission. The pivaloyl linker (2) was found to cleave with high yields and purities the acids in various solvents (THF, CH2Cl2, dioxane, DMSO) by irradiation with light above 320 nm. Using this linker, we have demonstrated the solid-phase synthesis of test compounds by peptide synthesis, palladium-catalyzed cross coupling, and epoxidation. The linker proved to be stable toward the treatment with acids and bases. The photolysis rates of our pivaloyl linker (2) were compared with the rates of a o- nitrobenzyl photolinker (1) and proved to be superior.
Peptide synthesis on fluorous support
Mizuno, Mamoru,Goto, Kohtaro,Miura, Tsuyoshi,Matsuura, Takeshi,Inazu, Toshiyuki
, p. 3425 - 3428 (2004)
New fluorous supports were synthesized and used to prepare a peptide having a C-terminal COOH based on fluorous chemistry. The hexakisfluorous chain-type support was suitable for the synthesis of a pentapeptide or a peptide derivative on a fluorous support whose fluorine content is over 40 w/w%. A bioactive peptide, Leu-enkephalin, was easily synthesized using an Fmoc-strategy based on fluorous chemistry.
Sustainable Peptide Synthesis Enabled by a Transient Protecting Group
Avrutina, Olga,Knauer, Sascha,Koch, Niklas,Kolmar, Harald,Meusinger, Reinhard,Uth, Christina
supporting information, p. 12984 - 12990 (2020/06/01)
The growing interest in synthetic peptides has prompted the development of viable methods for their sustainable production. Currently, large amounts of toxic solvents are required for peptide assembly from protected building blocks, and switching to water as a reaction medium remains a major hurdle in peptide chemistry. We report an aqueous solid-phase peptide synthesis strategy that is based on a water-compatible 2,7-disulfo-9-fluorenylmethoxycarbonyl (Smoc) protecting group. This approach enables peptide assembly under aqueous conditions, real-time monitoring of building block coupling, and efficient postsynthetic purification. The procedure for the synthesis of all natural and several non-natural Smoc-protected amino acids is described, as well as the assembly of 22 peptide sequences and the fundamental issues of SPPS, including the protecting group strategy, coupling and cleavage efficiency, stability under aqueous conditions, and crucial side reactions.
Exploration of the fifth position of leu-enkephalin and its role in binding and activating delta (DOP) and mu (MOP) opioid receptors
Ndong, Dominique Bella,Blais, Véronique,Holleran, Brian J.,Proteau-Gagné, Arnaud,Cantin-Savoie, Isabelle,Robert, William,Nadon, Jean-Fran?ois,Beauchemin, Sophie,Leduc, Richard,Pi?eyro, Graciela,Guérin, Brigitte,Gendron, Louis,Dory, Yves L.
, (2019/03/21)
Enkephalins are pentapeptidic endogenous ligands that regulate nociception by binding to mu (MOP) and delta (DOP) opioid receptors. To further explore the role of the leucine residue of Leu-enkephalin, 12 peptidomimetic analogs were synthesized by systematically replacing this residue with non-natural amino acids. The analogs were tested for their ability to bind DOP and MOP. We also investigated the potency of these analogs to inhibit cAMP production and to recruit β-arrestin 2 via both receptors. We found that replacement of the leucine residue by substituted non-natural amino acid derivatives of alanine, cycloleucine, or isoleucine was generally well tolerated. By contrast, substituting leucine with homoproline greatly reduced the affinity for DOP and, to a lesser extent, for MOP. Interestingly, when compared to Leu-enkephalin, analogs containing either aza-β-homoleucine or cycloleucine showed a bias toward inhibition of cAMP production through the activation of DOP but not MOP. By contrast, derivatives containing 4,5-dehydroleucine orD-allo-isoleucine conferred a bias toward β-arrestin 2 at MOP, but not DOP. Our results suggest that position 5 in Leu-enkephalin analogs can be further exploited to develop compounds with the potential to produce bias toward G protein or β-arrestin 2.