311345-45-6

Upstream product

• 93250-96-5 (2R,4S)-methyl 4-allyl-2-tert-butyl-3-formyloxazolidine-4-carboxylate 

Downstream Products

• 208837-91-6 (S)-methyl 2-(benzyloxycarbonylamino)-2-(hydroxymethyl)pent-4-enoate 
• 478945-06-1 2-amino-2-(tert-butyl-diphenyl-silanyloxymethyl)-pent-4-enoic acid methyl ester 
• 311345-38-7 (S) 2-[4-(4-Fluoro-phenoxy)-benzenesulfonylamino]-2-hydroxymethyl-pent-4-enoic acid methyl ester 
• 1015251-60-1 (S)-methyl 2-(benzyloxycarbonylamino)-2-formylpent-4-enoate 

Relevant academic research and scientific papers

Two phenyls are better than one or three: Synthesis and application of terminal olefin-oxazoline (TOlefOx) ligands

A novel terminal olefin-oxazoline ligand was introduced into rhodium-catalyzed asymmetric conjugate addition of arylboronic acids to enones and gave excellent enantioselectivities. The two phenyls proved better than one or three in ligand evaluations.

New fast and practical method for the enantioselective synthesis of α-vinyl, α-alkyl quaternary α-amino acids

We describe a fast and practical enantioselective synthesis of (S)-N-Cbz-α-vinyl, phenylalanine, suitable for the preparation of different N-Cbz-α-vinyl aminoacids of both configurations. The new protocol exploits a Wittig reaction on highly enantiomeric enriched N-Cbz-α-formyl-α-alkyl amino esters, readily accessible from (l)-serine through a stereoselective alkylation of Seebach's oxazolidine, carried out with a significant improvement of the previously reported method. The synthetic scheme is suitable for gram scale preparation of the desired product with a 94% ee.

Stereoselective synthesis of amino-substituted apio dideoxynucleosides through a distant neighboring group effect

Novel amino-substituted apio nucleoside (2R,4R)-LJ-45 as a potential anti-HBV agent was stereoselectively synthesized from the known oxazolidine 1 through a distant neighboring group effect. It is believed that this synthetic method using a chiral template, (-)-L-serine methyl ester can be generally applied to the synthesis of other chiral amino-substituted nucleosides.

Bicyclic metabotropic glutamate receptor ligands

The present invention provides bicyclic metabotropic glutamate receptor ligands, as well as compositions comprising such ligands, and and methods for their use.

Synthesis and biology of the conformationally restricted ACPD analogue, 2-aminobicyclo[2.1.1]hexane-2,5-dicarboxylic Acid-I, a potent mGluR agonist

To better characterize the roles of metabotropic glutamate receptors (mGluRs) in physiological and pathophysiological processes, there is an important need to learn more about the structural features relevant to the design of novel, high-affinity ligands that are family and subtype specific. To date, many of the biological studies that have been conducted in the area of mGluR research have made use of the agonist (1S,3R)-ACPD. This compound has been shown to act as an agonist at both the group I and group II receptors while showing little selectivity among the four subtypes belonging to these two groups. Moreover, (1S,3S)-ACPD, the cis isomer, shows negligible activity at group I receptors and is a good agonist of mGluR2. Since ACPD is itself somewhat flexible, with four distinctive conformations being identified from molecular modeling studies for the trans isomer and five conformations for the cis isomer, we believed that it would be of interest to examine the activity of an ACPD analogue that has been constrained through the introduction of a single carbon atom bridge. Accordingly, we have prepared an aminobicyclo[2.1.1]hexanedicarboxylic acid (ABHxD-I) analogue of ACPD. The synthesis of this compound was accomplished by use of an intramolecular [2 + 2] photocycloaddition reaction, in which four distinct isomers were isolated. Of these four compounds, only a single isomer, ABHxD- I (6a), was found to be a potent agonist of the mGluRs. This compound, which expresses the fully extended glutamate conformation, was found to be more potent than ACPD at all six of the eight mGluR subtypes that were investigated and to be comparable to or more potent than the endogenous ligand, glutamate, for these receptors. Interestingly, despite its fixed conformation, ABHxD-I, like glutamate, shows little subtype selectivity. Through modeling studies of ABHxD-I (6a), ABHD-VI, LY354740, (1S,3R)-ACPD, (1S,3S)-ACPD, and L-glutamate, we conclude that the aa conformation of L- glutamate is the active conformation for both group I and group II mGluRs. Moreover, the modeling-based comparisons of these ligands suggest that the selectivity exhibited by LY354740 between the group I and group II mGluRs is not a consequence of different conformations of L-glutamate being required for recognition at these mGluRs but rather is related to certain structural elements within certain regions having a very different impact on the group I and group II mGluR activity. The enhanced potency of ABHxD-I relative to trans-ACPD commends it as a useful starting point in the design of subtype selective mGluR ligands.