An improved protocol for the preparation of (S)-vinylglycine from (S)-methionine

Küchenthal, Christian-H.; Migenda, Julia; Polednia, Magdalena; Maison, Wolfgang

doi:10.1007/s00726-009-0460-3

Cited by 5 publications

(3 citation statements)

References 57 publications

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“…The earlier unknown D -Glu-γ-P H ( 1 ) may be prepared chemically (Fig. 2 ) and key precursor is methyl N -Cbz- D -vinylglycine ( 2 ), which can be synthesised following the protocols developed and used for the corresponding L -isomer 32 . To prepare methyl N -Cbz- L -vinylglycine different starting compounds, including amino acids, were used and reported elsewhere 32 and many of these synthetic approaches may be directly applied to prepare ( 2 ).…”

Section: Resultsmentioning

confidence: 99%

“…2 . Pathway (D), starting from D -Met, follows a classical and widely used 3-step Rapoport synthesis 32 . Alternatively, ( 2 ) can be prepared from commercially available D -3-aminobutyrolactone hydrochloride ( 3 ) in six steps, either following pathway (C) via selenide ( 4 ) 33 or via sulfoxide ( 5 ), following pathway (B), which also consists of six steps 34 .…”

Section: Resultsmentioning

confidence: 99%

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Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group

et al. 2020

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Escherichia coli glutamate decarboxylase (EcGadB), a pyridoxal 5'-phosphate (PLP)-dependent enzyme, is highly specific for L-glutamate and was demonstrated to be effectively immobilised for the production of γ-aminobutyric acid (GABA), its decarboxylation product. Herein we show that EcGadB quantitatively decarboxylates the L-isomer of D,L-2-amino-4-(hydroxyphosphinyl)butyric acid (D,L-Glu-γ-P H), a phosphinic analogue of glutamate containing C-P-H bonds. This yields 3-aminopropylphosphinic acid (GABA-P H), a known GABA B receptor agonist and provides previously unknown D-Glu-γ-P H , allowing us to demonstrate that L-Glu-γ-P H , but not D-Glu-γ-P H , is responsible for D,L-Glu-γ-P H antibacterial activity. Furthermore, using GABase, a preparation of GABA-transaminase and succinic semialdehyde dehydrogenase, we show that GABA-P H is converted to 3-(hydroxyphosphinyl)propionic acid (Succinate-P H). Hence, PLP-dependent and NADP +-dependent enzymes are herein shown to recognise and metabolise phosphinic compounds, leaving unaffected the P-H bond. We therefore suggest that the phosphinic group is a bioisostere of the carboxyl group and the metabolic transformations of phosphinic compounds may offer a ground for prodrug design.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group

et al. 2020

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“…Following a known protocol, we started our synthesis with enantiomerically pure Cbz-(S)-vinylglycine (3), which is readily available by a two-step synthesis from Cbz-(S)-methionine (2). 23 In parallel, dibenzyl glutarate (5) was prepared from benzyl acrylate (4) via a Baylis-Hilman type reaction with (n-Bu) 3 P. 24 Addition of ammonium hypophosphite gave phosphinic acid 6 as a racemate. Following a protocol of Vitharana et al, 25 stepwise crystallization with first yohimbine and second (S)-methylbenzylamine gave (S)-6 and (R)-6 in 31 and 28% yield, respectively over two steps.…”

Section: Resultsmentioning

confidence: 99%

Synthesis of dipeptide mimics based on amino phosphinate backbones and cyclic derivatives

Rüping¹,

Küchenthal²,

Maison³

2015

Arkivoc

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Dialkyl phosphinates are valuable peptide mimics for metallopeptidase targets. Despite their large pharmaceutical potential, the synthesis of many phosphinates remains challenging. An additional drawback for many applications is the high polarity of the phosphinate group. Herein we describe the synthesis of stereoisomerically pure GPI (1), a phosphinate with high binding affinity for the cancer specific zinc peptidase PSMA (prostate specific membrane antigen). In addition, analogous cyclic phosphinate esters 13, 16 and 23 are reported that might be useful as less polar ligands for metallo peptidase binding. The key step to these new 1,2-oxaphosphorinan-2-ones is an intramolecular cyclization of an intermediate H-phosphinate. The cyclizations work with modest diastereoselectivities of ~2:1 in favor of the trans arrangement of substituents at 2-and 4-position of the 1,2-oxaphosphorinan-2-one scaffolds.

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Site Covalent Modification of Methionyl Peptides for the Production of FRET Complexes

Jadhav

Shen

Sammynaiken

et al. 2015

Chemistry A European J

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Flax cyclic peptides (orbitides, linusorbs (LOs)) [1-8-NαC],[1-MetO2]-linusorb B1 ([MetO2]-LO1) and [1-9-NαC],[1-MetO2]-linusorb B2 ([MetO2]-LO2) are biologically active. These LOs lack active nuclei commonly used in peptide modification. We have developed reactions to activate methionine methyl sulphide to produce stable derivatives. In these reactions, LOs are converted to sulfonium intermediates and subsequently to derivatives containing active nuclei while preserving their fundamental structures. The reaction conditions preserved cyclic peptide fundamental structure and organic solvent solubility. [Met]-LO1 and [Met]-LO2 analogues containing activated groups (-CN, -COOEt, and -NH2 ) in the form of methionine, methionine (S)-oxide, and methionine (S,S)-dioxide amino acids were synthesized and characterized by LCMS and 1D and 2D NMR spectroscopy. Coumarin orbitide complexes produced in this manner bind Eu(3+) yielding FRET compounds that absorb energy through coumarin antennae and emit photons at lanthanide wavelengths.

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An improved protocol for the preparation of (S)-vinylglycine from (S)-methionine

Cited by 5 publications

References 57 publications

Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group

Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group

Synthesis of dipeptide mimics based on amino phosphinate backbones and cyclic derivatives

Site Covalent Modification of Methionyl Peptides for the Production of FRET Complexes

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