145038-52-4

Basic information

• Product Name: FMOC-ASP-OME
• Synonyms: FMOC-ASP-OME;FMOC-L-ASP-OME;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-L-ASPARTIC ACID ALPHA-METHYL ESTER;Fmoc-L-Aspartic acid methyl ester;N-ALPHA-(9-FLUOROENYLMETHYLOXYCARBONYL)-L-ASPARTIC ACID ALPHA-METHYL ESTER;(S)-3-(((9H-fluoren-9-yl)methoxy)carbonylamino)-4-methoxy-4-oxobutanoic acid;Fmoc-L-aspartic acid alpha methyl ester;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-aspartic acid 1-methyl ester
• CAS NO: 145038-52-4
• Molecular Formula: C20H19NO6
• Molecular Weight: 369.37
• Product Categories: Fmoc-Amino Acids and Derivatives;Fmoc-Amino acid series
• Mol File: 145038-52-4.mol

Chemical Properties

• Boiling Point: 609.7 °C at 760 mmHg
• Flash Point: 322.5 °C
• Appearance: /
• Density: 1.322±0.06 g/cm3 (20 ºC 760 Torr)
• Refractive Index: 1.596
• Storage Temp.: 2-8°C
• PKA: 4.05±0.19(Predicted)
• CAS DataBase Reference: FMOC-ASP-OME(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-ASP-OME(145038-52-4)
• EPA Substance Registry System: FMOC-ASP-OME(145038-52-4)

Safety Data

• Hazardous Substances Data: 145038-52-4(Hazardous Substances Data)

Usage

Uses

Used in Peptide Synthesis:
FMOC-ASP-OME is used as a building block for the synthesis of aspartic acid-containing peptides. Its role is vital in the construction of complex peptide structures, which are essential for various biological and pharmaceutical applications. The presence of protecting groups allows for controlled synthesis, ensuring the desired peptide sequence is achieved without unwanted side reactions.
Used in Organic Chemistry Research:
In the realm of organic chemistry, FMOC-ASP-OME is utilized for research purposes, exploring its properties and potential applications. Its unique structure, with both FMOC and OME protecting groups, makes it an interesting subject for studying the effects of protecting groups on peptide synthesis and the development of new synthetic methods.
Used in Pharmaceutical Development:
FMOC-ASP-OME contributes to the development of pharmaceuticals by enabling the synthesis of specific peptides with therapeutic potential. These peptides can be designed to target various diseases and conditions, offering new treatment options and advancing the field of medicine.
Used in Commercial Research and Laboratory Applications:
FMOC-ASP-OME is commercially available for research and laboratory use, providing scientists and researchers with a reliable source of this essential compound. Its availability facilitates ongoing research and development in peptide synthesis and organic chemistry, driving innovation and discovery in these fields.

InChI:InChI=1/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

Upstream product

• 71989-14-5 Fmoc-(tBu)Asp-OH 
• 172846-53-6 4-(tert-butyl) 1-methyl (((9H-fluoren-9-yl)methoxy)carbonyl)-L-aspartate 
• 177609-12-0 N-alpha-(9-fluorenylmethyloxycarbonyl)-D-aspartic acid beta-allyl ester 
• 368443-81-6 α-methyl γ-allyl (2R)-N-(fluoren-9-ylmethoxycarbonyl)aspartate 

Relevant articles and documents

Synthesis of chlorophyll-amino acid conjugates as models for modification of proteins with chromo/fluorophores

A chlorophyll-a derivative bonded directly with epoxide at the peripheral position of the chlorin π-system was reacted with N-urethane and C-ester protected amino acids bearing an alcoholic or phenolic hydroxy group as well as a carboxy group at the residue to give chlorophyll-amino acid conjugates. The carboxy residues of N,C-protected aspartic and glutamic acids were esterified with the epoxide in high yields. The synthetic conjugates in dichloromethane had absorption bands throughout the visible region including intense red-side Qy and blue-side Soret bands. By their excitation at the visible bands, strong and efficient fluorescence emission was observed up to the near-infrared region. The chromo/fluorophores are promising for preparation of functional peptides and modification of proteins.

Rhodium(I) and Iridium(I) N-Heterocyclic carbene complexes of imidazolium functionalized amino acids and peptides

The conjugation of organometallic complexes to peptides is generally achieved through covalent organic linkages of the metal's ligand to the peptide. Examples of direct coordination to metal centers by amino acid side chain residues remain rare. In one such example, side chain methylation of the natural amino acid histidine (His) resulted in an imidazolium functionalized amino acid which was used for the synthesis of rhodium(I), iridium(I), iridium(III), palladium(II) and ruthenium(III) N-heterocyclic carbene (NHC) complexes of the single amino acid and peptides containing this amino acid. Here, we have synthesized two new, non-natural imidazolium functionalized amino acid derivatives, which were used for solid phase peptide synthesis and for the synthesis of [M(COD)(NHC)Cl] (COD = 1,5 cyclooctadiene) complexes of Rh(I) and Ir(I). In total, six new complexes of the single amino acids and four complexes where the amino acids are present in a peptide environment were synthesized. Their characterization provides convincing evidence of conversion of the imidazolium moiety to an NHC ligand and thus the presence of a direct metal-carbon bond between the metal center and the amino acid side chain. Therefore, our compounds represent unique examples of peptide-conjugated complexes that bear the potential to be used for the synthesis of N-heterocyclic carbene complexes conjugated to cancer cell targeting peptides.

Hydantoin and thiohydantoin derivatives as antiviral drugs

The present invention relates to a compound of the following formula (I), or a salt, solvate, tautomer, enantiomer, diastereoisomer or racemic mixture thereof: as well as its use as a drug, notably in the treatment of hepatitis C, its preparation process, and the pharmaceutical compositions containing such a compound.

HYDANTOIN AND THIOHYDANTOIN DERIVATIVES AS ANTIVIRAL DRUGS

The present invention relates to a compound of the following formula (I), or a salt, solvate, tautomer, enantiomer, diastereoisomer or racemic mixture thereof: as well as its use as a drug, notably in the treatment of hepatitis C, its preparation process, and the pharmaceutical compositions containing such a compound.

Design and preparation of serine-threonine protein phosphatase inhibitors based upon the nodularin and microcystin toxin structures. Part 3

Nodularin and microcystins are complex natural cyclic isopeptidic hepatotoxins that serve as subnanomolar inhibitors of the eukaryotic serine-threonine protein phosphatases PP1 and PP2A, enzymes that are intimately involved in controlling cellular metabolism. Previously we described a solution-phase synthesis of stripped-down nodularin analogues; cyclo[-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)-Asp-α-OMe- β-(S)-Phe-] 3 and cyclo[-(3R)-3-hydroxymethyl-β-Ala-(R)-Glu-α-OMe-γ-Sar-(R)- Asp-α-OMe-β-(S)-Phe-] 5. The synthetic strategy was designed to allow post-macrocyclisation elaboration. Here we examine alternative methods for introducing diversity and achieving macrolactamisation and compare the relative efficiency of solution- vs. solid-phase peptide syntheses of the macrocycles. Syntheses and the biological activities of the macrocycles cyclo{-[(2R)-α-4-benzylpiperidinylamido-Asp]-β-[(R)-Glu]-γ- Sar-[(R)-Asp]-β-(S)-Phe-} 29 and cyclo{-(2S)-Phe-[(2R)-α-4-benzylpiperidinylamido-Asp]-(R)-Glu-γ- (S)-Pro-β-(R)-Asp-} 65 are compared. Both compounds contain sufficient side-chain functionality to interact with a hydrophobic groove at the enzyme active site. The proline containing analogues 30, 31 (R3 = CH3) where sarcosine is replaced in macrocycles 3 and 4, were also synthesised in order to correlate conformational properties with biological activity. In accord with predictions macrocycles 29 and 65 were found to be weak inhibitors of PP1 with IC50 2.9 and 2.7 mM respectively.

Nu-alloc temporary protection in solid-phase peptide synthesis. The use of amine-borane complexes as allyl group scavengers

The use of a combination of amine-borane complexes and soluble palladium catalyst allows the fast deprotection of allyl carbamates under near-to-neutral conditions and without any side-formation of allylamine. Preliminary experiments: indicate that palladium catalyst-amine-borane systems seem ideally suited for removal of Nu-Alloc terminal groups during solid phase peptide synthesis according to the Nu-Alloc temporary protection strategy. The Royal Society of Chemistry 1999.

New Allyl Group Acceptors for Palladium Catalyzed Removal of Allylic Protections and Transacylation of Allyl Carbamates.

Key words: allylic protecting groups, palladium catalysis, transacylation, phenyltrihydrosilane, N-methyl-N-(trimethylsilyl)trifluoroacetamide.Allyl carboxylates, carbamates and phenoxides may be cleaved or transacylated in the presence of palladium catalyst and either phenyltrihydridosilane or N-methyl-N-(trimethylsilyl)trifluoroacetamide.These reactions are totally compatible with the presence of Boc and, as far as phenyltrihydrosilane is concerned, Fmoc protections.