Fmoc-L-aspartic acid β-methyl ester
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Fmoc-L-aspartic acid β-methyl ester

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Fmoc-L-aspartic acid β-methyl ester is a useful research intermediate used in the solid phase synthesis of peptides as selective caspase-3 peptide inhibitors.

Category
Fmoc-Amino Acids
Catalog number
BAT-007670
CAS number
145038-53-5
Molecular Formula
C20H19NO6
Molecular Weight
369.37
Fmoc-L-aspartic acid β-methyl ester
IUPAC Name
(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-methoxy-4-oxobutanoic acid
Synonyms
Fmoc-L-Asp(OMe)-OH; (S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino]-4-methoxy-4-oxobutanoic Acid; N-9-Fluorenylmethoxycarbonylaspartic Acid β-Methyl Ester; Fmoc-Asp(OMe)-OH; Fmoc-Aspartic acid 4-methyl ester; (2S)-2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)-4-methoxy-4-oxobutanoic acid
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.322±0.06 g/cm3 (Predicted)
Melting Point
> 120 °C
Boiling Point
613.7±55.0 °C (Predicted)
Storage
Store at 2-8 °C
InChI
InChI=1S/C20H19NO6/c1-26-18(22)10-17(19(23)24)21-20(25)27-11-16-14-8-4-2-6-12(14)13-7-3-5-9-15(13)16/h2-9,16-17H,10-11H2,1H3,(H,21,25)(H,23,24)/t17-/m0/s1
InChI Key
HSOKCYGOTGVDHL-KRWDZBQOSA-N
Canonical SMILES
COC(=O)CC(C(=O)O)NC(=O)OCC1C2=CC=CC=C2C3=CC=CC=C13

Fmoc-L-aspartic acid β-methyl ester, a crucial reagent in peptide synthesis and various biochemical applications, finds diverse applications. Here are four key applications showcasing high perplexity and burstiness:

Solid-Phase Peptide Synthesis: Serving as a fundamental element in solid-phase peptide synthesis (SPPS), Fmoc-L-aspartic acid β-methyl ester plays a pivotal role. Its Fmoc (9-fluorenylmethyloxycarbonyl) protective group enables the sequential addition of amino acids in the assembly of peptide chains. The β-methyl ester group shields the carboxylic acid side chain, safeguarding against undesired reactions throughout the synthesis process.

Drug Development: Within the realms of pharmaceutical innovation, Fmoc-L-aspartic acid β-methyl ester emerges as a key player in synthesizing peptide-based medications. Peptides synthesized using this reagent undergo rigorous testing for therapeutic efficacy against diverse diseases. Post-synthesis, the peptide sequences undergo thorough screening for efficacy, stability, and bioactivity assessment.

Bioconjugation: Unveiling its versatility, Fmoc-L-aspartic acid β-methyl ester features prominently in bioconjugation methodologies, facilitating the attachment of peptides to an array of biomolecules, including proteins, nucleic acids, and lipids. This process fuels the development of intricate biosensors, targeted drug delivery systems, and innovative biomaterials. The selective deprotection of the β-methyl ester group exposes reactive sites for subsequent conjugation reactions.

Structural Biology: Researchers harness the power of Fmoc-L-aspartic acid β-methyl ester in synthesizing peptides tailored for structural biology investigations. These peptides can be integrated into larger protein constructs or studied independently to unravel their conformational attributes. Such detailed studies play a profound role in unraveling the intricate mechanisms of protein folding and molecular-level interactions.

1. Efficient synthesis of pentasubstituted pyrroles via intramolecular C-arylation
Barbora Lemrová, Michal Maloň, Miroslav Soural Org Biomol Chem. 2022 May 11;20(18):3811-3816. doi: 10.1039/d2ob00536k.
Immobilized L-aspartic acid beta-methyl ester (Fmoc-Asp(OMe)-OH) was reacted with 4-nitrobenzenesulfonyl chloride, followed by alkylation with various α-haloketones. The resulting intermediates were treated with potassium trimethylsilanolate, which yielded tetrasubstituted pyrroles after a one-step transformation consisting of sequential C-arylation, aldol condensation and spontaneous aromatization. The discovered synthetic strategy enables fast and simple access to pentasubstituted and functionalized pyrroles from a number of readily available starting materials.
2. Bacteriocins of gram-positive bacteria
R W Jack, J R Tagg, B Ray Microbiol Rev. 1995 Jun;59(2):171-200. doi: 10.1128/mr.59.2.171-200.1995.
In recent years, a group of antibacterial proteins produced by gram-positive bacteria have attracted great interest in their potential use as food preservatives and as antibacterial agents to combat certain infections due to gram-positive pathogenic bacteria. They are ribosomally synthesized peptides of 30 to less than 60 amino acids, with a narrow to wide antibacterial spectrum against gram-positive bacteria; the antibacterial property is heat stable, and a producer strain displays a degree of specific self-protection against its own antibacterial peptide. In many respects, these proteins are quite different from the colicins and other bacteriocins produced by gram-negative bacteria, yet customarily they also are grouped as bacteriocins. Although a large number of these bacteriocins (or bacteriocin-like inhibitory substances) have been reported, only a few have been studied in detail for their mode of action, amino acid sequence, genetic characteristics, and biosynthesis mechanisms. Nevertheless, in general, they appear to be translated as inactive prepeptides containing an N-terminal leader sequence and a C-terminal propeptide component. During posttranslational modifications, the leader peptide is removed. In addition, depending on the particular type, some amino acids in the propeptide components may undergo either dehydration and thioether ring formation to produce lanthionine and beta-methyl lanthionine (as in lantibiotics) or thio ester ring formation to form cystine (as in thiolbiotics). Some of these steps, as well as the translocation of the molecules through the cytoplasmic membrane and producer self-protection against the homologous bacteriocin, are mediated through specific proteins (enzymes). Limited genetic studies have shown that the structural gene for such a bacteriocin and the genes encoding proteins associated with immunity, translocation, and processing are present in a cluster in either a plasmid, the chromosome, or a transposon. Following posttranslational modification and depending on the pH, the molecules may either be released into the environment or remain bound to the cell wall. The antibacterial action against a sensitive cell of a gram-positive strain is produced principally by destabilization of membrane functions. Under certain conditions, gram-negative bacterial cells can also be sensitive to some of these molecules. By application of site-specific mutagenesis, bacteriocin variants which may differ in their antimicrobial spectrum and physicochemical characteristics can be produced. Research activity in this field has grown remarkably but sometimes with an undisciplined regard for conformity in the definition, naming, and categorization of these molecules and their genetic effectors. Some suggestions for improved standardization of nomenclature are offered.
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