N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester
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N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester

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Category
CBZ-Amino Acids
Catalog number
BAT-005985
CAS number
35909-93-4
Molecular Formula
C14H17NO6
Molecular Weight
295.29
N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester
IUPAC Name
dimethyl (2S)-2-(phenylmethoxycarbonylamino)butanedioate
Synonyms
Z-Asp(OMe)-OMe
InChI
InChI=1S/C14H17NO6/c1-19-12(16)8-11(13(17)20-2)15-14(18)21-9-10-6-4-3-5-7-10/h3-7,11H,8-9H2,1-2H3,(H,15,18)/t11-/m0/s1
InChI Key
YPDSGUUJTVECEP-NSHDSACASA-N
Canonical SMILES
COC(=O)CC(C(=O)OC)NC(=O)OCC1=CC=CC=C1

N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester, a chemical compound with diverse applications in bioscience and pharmaceuticals, serves as a versatile tool in various domains. Below are four key applications of N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester, presented with high perplexity and burstiness:

Peptide Synthesis: In the realm of peptide synthesis, N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester plays a pivotal role as a protected amino acid derivative. By incorporating protective groups, it safeguards against undesired side reactions during the elongation of peptide chains. This meticulous process ensures the precise assembly of intricate peptides, critical in the realms of drug development and biochemical research.

Protein Engineering: Delving into the domain of protein engineering, this compound emerges as a valuable asset, facilitating the modification of protein structures. Through the integration of modified amino acids, scientists delve into the realms of protein folding, stability, and functionality. This profound understanding is paramount in the creation of proteins endowed with enhanced therapeutic attributes or industrial applications.

Drug Delivery Systems: Embarking on the frontier of drug delivery innovations, N-α-Carbobenzoxy-L-aspartic acid α,β-dimethyl ester finds its utility in the development of avant-garde drug delivery systems. Serving as a foundational unit in the construction of biodegradable polymers, it enables the encapsulation of drugs for controlled release. This sophisticated mechanism enhances the efficacy and safety of medications, paving the way for advanced therapeutic approaches.

Enzyme Inhibition Studies: Leading the charge in enzyme inhibition studies, researchers leverage this compound to delve into the intricate world of enzyme-substrate interactions. By introducing this derivative into enzyme assays, scientists unravel the impact of modifications on enzyme activity. These profound insights are instrumental in crafting specific inhibitors for therapeutic applications and unraveling the intricate pathways of metabolism.

1. In vitro anti-leishmanial activity of Prunus armeniaca fractions on Leishmania tropica and molecular docking studies
Nargis Shaheen, Naveeda Akhter Qureshi, Asma Ashraf, Aneeqa Hamid, Attiya Iqbal, Huma Fatima J Photochem Photobiol B. 2020 Dec;213:112077. doi: 10.1016/j.jphotobiol.2020.112077. Epub 2020 Nov 3.
Prunus armeniaca (L.) is a member of the Rosaceae, subfamily Prunoideae, shows anticancer, antitubercular, antimutagenic, antimicrobial, antioxidant, and cardioprotective activities. Here we fractionated the leaves extract of this highly medicinally important plant for antileishmanial activity. In the current study, the leaves extract was fractionated and characterized using column and thin layer chromatography by n-hexane, ethyl acetate, and methanol solvents. Twelve fractions were isolated and subjected for evaluation of their cytotoxicity and in vitro antileishmanial activity against promastigotes and amastigotes of Leishmania tropica. Among all fractions used, the fraction (F7) exhibited the strongest antileishmanial activity. The bioactive fraction was further characterized by spectroscopy (FTIR, UV-Vis), and GC-MS analysis. The in silico docking was carried out to find the active site of PTR1. All derived fractions exhibited toxicity in the safety range IC50 > 100 μg/ml. The fraction (F7) showed significantly the highest antipromastigotes activity with IC5011.48 ± 0.82 μg/ml and antiamastigotes activity with IC50 21.03 ± 0.98 μg/ml compared with control i.e. 11.60 ± 0.70 and 22.03 ± 1.02 μg/ml respectively. The UV-Vis spectroscopic analysis revealed the presence of six absorption peaks and the FTIR spectrum revealed the presence of alkane, aldehyde, carboxylic acid, thiols, alkynes, and carbonyls compounds The GC-MS chromatogram exhibited the presence of nine compounds: (a) benzeneethanol, alpha, beta dimethyl, (b)carbazic acid, 3-(1 propylbutylidene)-, ethyl ester, (c)1, 2-benzenedicarboxylic acid, diisooctyl ester, (d)benzeneethanamine a-methyl, (e)2aminononadecane, (f)2-heptanamine-5-methyl, (g)cyclobutanol, (h)cyclopropyl carbine, and (i)nitric acid, nonyl ester. Among all compounds, the 1, 2-benzenedicarboxylic acid, diisooctyl ester bound well to the PTR1 receptor. Fraction (F7) showed acceptable results with no cytotoxicity. However, in vivo studies are required in the future.
2. Specificity and formation of unusual amino acids of an amide ligation strategy for unprotected peptides
J P Tam, C Rao, C F Liu, J Shao Int J Pept Protein Res. 1995 Mar;45(3):209-16. doi: 10.1111/j.1399-3011.1995.tb01482.x.
An important step in the recently developed ligation strategy known as domain ligation strategy to link unprotected peptide segments without activation is the ring formation between the C-terminal ester aldehyde and the N-terminal amino acid bearing a beta-thiol or beta-hydroxide. A new method was developed to define the specificity of this reaction using a dye-labeled alanyl ester aldehyde to react with libraries of 400 dipeptides which contained all dipeptide combinations of the 20 genetically coded amino acids. Three different ester aldehydes of the dye-labeled alanine: alpha-formylmethyl (FM), beta-formylethyl (FE), and beta,beta,beta-dimethyl and formylethyl esters (DFE), were examined. The DFE ester was overly hindered and reacted with N-terminal Cys dipeptides (Cys-X). Interestingly, it also reacted slowly with the sequences of X-Gly where Gly was the second amino acid and the X-Gly amide bond participated in the ring formation. Although the FE ester reacted similarly as the FM ester in the ring formation, the subsequent O,N-acyl transfer was at least 30-fold slower than those of the FM-ester. The FM alpha-formyl methyl ester was the most suitable ester and was reactive with dipeptides of six N-terminal amino acids: Cys, Thr, Trp, Ser, His and Asn. The order and extent of their reactivity were highly dependent on pH, solvent and neighboring participation by the adjacent amino acid. In general, they could be divided into three categories. (1) N-Terminal Cys and Thr were the most reactive.(ABSTRACT TRUNCATED AT 250 WORDS)
3. Correlation between serum levels of some cholesterol precursors and activity of HMG-CoA reductase in human liver
I Björkhem, T Miettinen, E Reihnér, S Ewerth, B Angelin, K Einarsson J Lipid Res. 1987 Oct;28(10):1137-43.
The possibility that the serum concentrations of various cholesterol precursors may reflect the activity of the hepatic HMG-CoA reductase was investigated in humans under different conditions. The serum levels of squalene, free and esterified lanosterol, (4 alpha, 4 beta, 14 alpha-trimethyl-5 alpha-cholest-8, 24-dien-3 beta-ol), two dimethylsterols (4 alpha, 4 beta-dimethyl-5 beta-cholest-8-en-3 beta-ol and 4 alpha, 4 beta-dimethyl-5 alpha-cholest-8, 24-dien-3 beta-ol), two methostenols (4 alpha-methyl-5 alpha-cholest-7-en-3 beta-ol and 4 alpha-methyl-5 alpha-cholest-8-en-3 beta-ol), two lathosterols (5 alpha-cholest-7-en-3 beta-ol and 5 alpha-cholest-8-en-3 beta-ol) and desmosterol (cholest-5, 24-dien-3 beta-ol) were measured in untreated patients (n = 7) and patients treated with cholestyramine (QuestranR, 8 g twice daily for 2-3 weeks, n = 5) or chenodeoxycholic acid (15 mg/kg body weight daily for 3-4 weeks, n = 8) prior to elective cholecystectomy. The activity of the hepatic microsomal HMG-CoA reductase was measured in liver biopsies taken in connection with the operation.(ABSTRACT TRUNCATED AT 250 WORDS)
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