104870-31-7

Basic information

• Product Name: L-Aspartic acid, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-a-aspartyl]-, tris(phenylmethyl) ester
• CAS NO: 104870-31-7
• Molecular Formula: C34H38N2O9
• Molecular Weight: 618.684
• Mol File: 104870-31-7.mol

Chemical Properties

• CAS DataBase Reference: L-Aspartic acid, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-a-aspartyl]-, tris(phenylmethyl) ester(CAS DataBase Reference)
• NIST Chemistry Reference: L-Aspartic acid, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-a-aspartyl]-, tris(phenylmethyl) ester(104870-31-7)
• EPA Substance Registry System: L-Aspartic acid, N-[N-[(1,1-dimethylethoxy)carbonyl]-L-a-aspartyl]-, tris(phenylmethyl) ester(104870-31-7)

Safety Data

• Hazardous Substances Data: 104870-31-7(Hazardous Substances Data)

Upstream product

• 13798-75-9 N^α-t-butoxycarbonylaspartic acid α-N-hydroxysuccinimide ester β-benzyl ester 
• 2886-33-1 dibenzyl L-aspartate toluene-4-sulphonate 
• 2791-79-9 dibenzyl L-aspartate 
• 7536-58-5 BOC-L-aspartic acid 4-benzyl ester 
• 6327-59-9 L-aspartic acid dibenzyl ester hydrochloride 

Downstream Products

• 118446-99-4 N^α-decanoyl-β-benzyl-L-aspartyl-L-aspartic acid dibenzyl ester 
• 107208-63-9 L-Asp-L-Asp-L-Asp-OH 
• 118429-75-7 dibenzyl (2S)-2-{[(2S)-2-amino-4-(benzyloxy)-4-oxobutanoyl]amino}butanedioate trifluoroacetate 
• 1421865-84-0 5’-O-[({(1S)-3-(benzyloxy)-1-[({(1S)-3-(benzyloxy)-1-[(benzyloxy)carbonyl]-3-oxopropyl}amino)carbonyl]-3-oxopropyl}amino)hydroxyphosphinyl]-2’-deoxyadenosine 
• 104870-33-9 Ac-Asp(OBzl)-Asp(OBzl)-OBzl 
• 118429-77-9 N^α-lauryl-β-benzyl-L-aspartyl-L-aspartic acid dibenzyl ester 

Relevant articles and documents

Solvent effects on the redox properties of ferrocenoyl-dipeptides

The preparation and characterization of the novel ferrocenoyl-dipeptides, Fc-Asp(OBzl)-Asp(OBzl)-OBzl (5), Fc-Asp(OBzl)-Glu(OEt)-OEt (6) and Fc-Asp(OBzl)-Cys(Bzl)-OMe (7) are reported. In addition, Fc-Asp(OBzl)-OBzl (4) and its free acid, Fc-Asp(OH)-OH (8), were prepared. A crystal structure determination of 8 revealed an extensive H-bonding network involving a solvent molecule and adjacent molecules of 8 and suggests that these complexes are able to form strong hydrogen bonds with solvent molecules. All compounds show reversible one-electron oxidations in solution. The half-wave potential is strongly influenced by the nature of the solvent and correlates with the hydrogen donor ability α of the Kamlet-Taft formalism.

PEPTIDE COMPOSITIONS FOR SLOWING DEGRADATION OF VITAMIN-MINERAL SUPPLEMENTS, FOODS, PHARMACEUTICALS, AND COSMETICS

Compositions of foods, vitamin and mineral supplements, topical or oral drugs, and cosmetic products containing a small peptide or peptides for slowing degradation, for example by transition metals. The peptides are di, tri, terra-, and/or penta-peptides

Dipeptides as leaving group in the enzyme-catalyzed DNA synthesis

Conjugates of 2′-deoxyadenosine monophosphate with dipeptides have been synthesized and tested as substrates for several polymerases. Although the incorporation efficiency is not very high, it demonstrates that some of these dipeptides can be accommodated in the active site of polymerases and function as leaving groups in the enzymatic synthesis of DNA. Copyright

Bone targeting prodrugs based on peptide dendrimers, synthesis and hydroxyapatite binding in vitro

Novel bone targeting naproxen prodrugs with poly(aspartic acid) moieties and with two and three poly(aspartic acid) sequences peptide dendrimers were synthesized using a conventional method. The modified naproxen conjugates were incubated with hydroxyapatite in PBS at physiological conditions over 16h. The study revealed the hydroxyapatite binding properties of poly(aspartic acid) and it was found that the peptide dendrimer prodrugs exhibited a faster initial binding and a greater total binding. The obtained binding data in vitro indicated that the peptide dendrimers with poly(aspartic acid) sequences were useful for the development of new bone targeting molecules for drug delivery to bone.

Synthesis of acyclic and dehydroaspartic acid analogues of Ac-Asp-Glu-OH and their inhibition of rat brain N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase)

The following structural and conformationally constrained analogues of Ac-Asp-Glu-OH (1) were synthesized: Ac-Glu-Glu-OH (2), Ac-D-Asp-Glu-OH (3), Ac-Glu-Asp-OH (4), Ac-Asp-Asp-OH (5), Ac-Asp-3-aminohexanedioic acid (6), Ac-3-amino-3-(carboxymethyl)propanoyl-Glu-OH (7), N-succinyl-Glu-OH (8), N-maleyl-Glu-OH (9), N-fumaryl-Glu-OH (10), and Ac-Δ(z)Asp-Glu-OH (11). These analogues were evaluated for their ability to inhibit the hydrolysis of Ac-Asp-[3,4-3H]-Glu-OH by N-acetylated α-linked acidic dipeptidase (NAALA dipeptidase) in order to gain some insight into the structural requirements for the inhibition of this enzyme. Analogues 4-6 and 9 were very weak inhibitors of NAALA dipeptidase (K(i) > 40 μM), while 2, 3, and 7 with K(i) values ranging from 3.2-8.5 μM showed intermediate inhibitory activity. The most active inhibitors of NAALA dipeptidase were compounds 8, 10, and 11 with K(i) values of 0.9, 0.4, and 1.4 μM, respectively. These results suggest that the relative spacing between the side chain carboxyl and the α-carboxyl group of the C-terminal residue may be important for binding to the active site of the enzyme. They also indicate that the χ1 torsional angle for the aspartyl residue is in the vicinity of 0°.

Fatty Acid Derivatives of Acidic Amino Acids as Potential Antibiotics

The synthesis of fatty acid derivatives (1-8) of acidic amino acids is reported and their bioactivity tested.At higher concentrations, these compounds cause denaturation of haemoglobin.None of these compounds inhibit E. coli growth up to 2.5 mg/ml.