171567-85-4

Usage

Uses

Used in Organic Chemistry:
D-Alanine, N-(methoxycarbonyl)(9CI) is used as a building block for the synthesis of various organic compounds due to its unique structure and reactivity.
Used in Medicinal Chemistry:
D-Alanine, N-(methoxycarbonyl)(9CI) is used as a key intermediate in the development of pharmaceuticals, particularly for the synthesis of peptide-based drugs, as its methoxycarbonyl group can influence the compound's properties and functions.
Used in Research and Development:
D-Alanine, N-(methoxycarbonyl)(9CI) is employed as a research tool in the study of amino acid derivatives and their potential applications in various fields, including drug discovery and material science.

Upstream product

• 1223-26-3 p-nitrophenyl N-methoxycarbonyl-D-phenylalaninate 
• 338-69-2 D-Alanine 
• 79-22-1 methyl chloroformate 

Relevant academic research and scientific papers

HEPATITIS C VIRUS INHIBITORS

The present disclosure relates to compounds, compositions and methods for the treatment of hepatitis C virus (HCV) infection. Also disclosed are pharmaceutical compositions containing such compounds and methods for using these compounds in the treatment of HCV infection.

Synthesis and antidepressant activity of optical isomers of 2-(4-benzylpiperazin-1-yl)-1-(5-chloro-6-methoxynaphthalen-2-yl) propan-1-ol (SIPI5056)

Four optical isomers of SIPI5056 were synthesized and evaluated for their antidepressant activities and acute toxicities as novel multiple reuptake inhibitors of monoamine transmitters. Chiral alanines were used as educts to prepare their respective target compounds in nine steps. Pharmacological results showed that the (1R,2S)-SIPI5056 isomer has higher inhibitory activity and lower toxicity than other three isomers and is worthy of further development.

HEPATITIS C VIRUS INHIBITORS

This disclosure concerns novel compounds of Formula (I) as defined in the specification and compositions comprising such novel compounds. These compounds are useful antiviral agents, especially in inhibiting the function of the NS5A protein encoded by Hepatitis C virus (HCV). Thus, the disclosure also concerns a method of treating HCV related diseases or conditions by use of these novel compounds or a composition comprising such novel compounds.

Hepatitis C Virus Inhibitors

This disclosure concerns novel compounds of Formula (I) as defined in the specification and compositions comprising such novel compounds. These compounds are useful antiviral agents, especially in inhibiting the function of the NS5A protein encoded by Hepatitis C virus (HCV). Thus, the disclosure also concerns a method of treating HCV related diseases or conditions by use of these novel compounds or a composition comprising such novel compounds.

HEPATITIS C VIRUS INHIBITORS

This disclosure concerns novel compounds of Formula (I) as defined in the specification and compositions comprising such novel compounds. These compounds are useful antiviral agents, especially in inhibiting the function of the NS5A protein encoded by Hepatitis C virus (HCV). Thus, the disclosure also concerns a method of treating HCV related diseases or conditions by use of these novel compounds or a composition comprising such novel compounds.

HEPATITIS C VIRUS INHIBITORS

The present disclosure relates to compounds of the following formula (I) or a pharmaceutically acceptable salt thereof, wherein A and B are each phenyl; D and E are each five-membered aromatic rings containing one, two, or three i hcteroatoms independently selected from nitrogen, oxygen, and sulfur; provided that ', at least one of D and E is other than imidazole; compositions and methods for the treatment of Hepatitis C virus (HCV) inf ection. Also disclosed are pharmaceutical compositions containing such compounds and methods f or using these compounds in the treatment of HCV inf ection.

An investigation of antibody acyl hydrolysis catalysis using a large set of related haptens

An aspect of catalytic antibody research that receives little attention in the literature involves hapten systems that fail to elicit antibody catalysts despite a high affinity immune response and hapten designs that resemble those known to elicit catalysts. We have investigated a series of 12 phosphate and phosphonate haptens in a total of three animal systems. Dramatic and reproducible differences were observed in the catalytic activities of polyclonal antibodies elicited by the different haptens. A phosphate hapten with a phenyl ring on the side of the hapten opposite the linker elicited reproducibly high levels of polyclonal antibody catalytic activity. The other 11 haptens, most with benzyl groups on the side of the hapten opposite the linker, elicited immune responses in which catalytic activity was significantly weaker in terms of the level of observed catalytic activity, as well as frequency of elicited catalysts. Our results indicate that subtle features of transition state analogue hapten structure can have a dramatic and reproducible influence over the catalytic activity of elicited antibodies in related haptens. Whatever the explanation, subtle changes in mechanistic features due to altered leaving group ability/location or overall hapten flexibility, the comprehensive data presented here indicate that phenyl or 4-nitrophenyl leaving groups located opposite the hapten linker are to be preferred in order to elicit highly active antibody catalysts for acyl hydrolysis reactions. (C) 2000 Elsevier Science Ltd.

Stereoselective Micellar Catalysis. Part 3. Co-operative Effects of N-Decanoyl-L-histidine for the Hydrolysis of Enantiomeric Substrates

The catalytic activities of N-decanoyl-L-histidine (Ia) and its methyl ester (Ib) toward the hydrolyses of enantiomeric substrates (II) have been investigated in the presence of cetyltrimethylammonium bromide micelles.The comparison of catalytic effects (both the rate constants and stereoselectivities) of (Ia) and (Ib) strongly suggests that carboxylate ion of (Ia) intramolecularly enhances the reactivity of the imidazole group.The presence of co-operative effects is also supported by the pH-rate profile and by the thermodynamic parameters of the reaction.