19653-58-8Relevant academic research and scientific papers
Single Electron Transfer-Induced Selective α-Oxygenation of Glycine Derivatives
Venugopal, Navyasree,Moser, Johannes,Vojtí?ková, Margaréta,Císa?ová, Ivana,K?nig, Burkhard,Jahn, Ullrich
supporting information, p. 405 - 412 (2021/11/03)
Modification of amino acids is an important strategy in organic and bioorganic chemistry. In contrast to common side-chain functionalization, backbone modification is much less explored. Especially glycine units seem to be attractive and versatile since a wide range of functionality can be potentially introduced. We report here oxidative modification of glycinates that are stable and enable further functionalization. Selective glycinate enolate oxidation by TEMPO or a FeCp2PF6/TEMPO reagent combination provides stable alkoxyamines in good to excellent yields. The methodology is expanded to glycine-containing dipeptides demonstrating selective oxygenation at the glycine unit. The orthogonal reactivity potential of oxygenated glycines for transformation to other amino acid derivatives is explored.
2-OXAMIDE INHIBITORS OF PHOSPHOLIPASE A2 ACTIVITY AND CELLULAR ARACHIDONATE RELEASE BASED ON DIPEPTIDES AND PSEUDOPEPTIDES
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Page/Page column 22, (2010/11/05)
The disclosure provides a series of 2-oxoamides based on dipeptides and pseudodipeptides, which were synthesized and their activities toward two human intracellular phospholipases A2 (GIVA CPLA2 and GVIA 1PLA2) and one human secretor
2-Oxoamide inhibitors of phospholipase A2 activity and cellular arachidonate release based on dipeptides and pseudodipeptides
Barbayianni, Efrosini,Stephens, Daren,Grkovich, Andrej,Magrioti, Victoria,Hsu, Yuan-Hao,Dolatzas, Panagiotis,Kalogiannidis, Dimitrios,Dennis, Edward A.,Kokotos, George
experimental part, p. 4833 - 4843 (2009/12/04)
A series of 2-oxoamides based on dipeptides and pseudodipeptides were synthesized and their activities towards two human intracellular phospholipases A2 (GIVA cPLA2 and GVIA iPLA2) and one human secretory phospholipase As
Unique sequence in deltorphin C confers structural requirement for δ opioid receptor selectivity
Lazarus, LH,Salvadori, S,Grieco, P,Wilson, WE,Tomatis, R
, p. 791 - 797 (2007/10/02)
A series of deltorphin C (H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues were synthesized to assess the consequences of changing anionic and hydrophobic residues on δ receptor selectivity.Analogues with altered C-terminal groups, inverted sequences, or es
4-Methoxy-2,3,6-trimethylbenzenesulfonyl (Mtr): a New Amino and Imidazole Protecting Group in Peptide Synthesis
Wakimasu, Mitsuhiro,Kitada, Chieko,Fujino, Masahiko
, p. 2766 - 2779 (2007/10/02)
The 4-methoxy-2,3,6-trimethylbenzenesulfonyl (Mtr) group was introduced as a protecting group for the amino function, especially the ε-amino function of lysine, and the imidazole ring of histidine.The Nε-Mtr group was removable by dilute methanesulfonic acid-containing trifluoroacetic acid-thioanisole, but was stable to trifluoroacetic acid or catalytic hydrogenation.The Nim-Mtr group was removable by trifluoroacetic acid-dimethylsulfide or 1-hydroxybenzotriazole, but was more stable than the Nim-Tos or the Nim-Mbs group with triethylamine.To examine the usefulness of the Mtr group as a protecting group for use in peptide synthesis, mastoparan X and chicken gastrin releasing peptide (c-GRP) were synthesized, and this group was found to be very convenient for general solution synthesis.In particular, the introduction of Lys(Mtr) made possible a new strategy in peptide synthesis.Keywords-4-methoxy-2,3,6-trimethylbenzenesulfonyl (Mtr); Nε-4-methoxy-2,3,6-trimethylbenzenesulfonyllysine; Nim-4-methoxy-2,3,6-trimethylbenzenesulfonylhistidine; methanesulfonic acid-trifluoroacetic acid-thioanisole deprotection; trifluoroacetic acid-dimethylsulfide deprotection; mastoparan X; chicken gastrin releasing peptide
