136092-80-3

Basic information

• Product Name: BOC-N-ME-ALLO-ILE-OH
• Synonyms: BOC-N-METHYL-L-ALLO-ISOLEUCINE;BOC-N-ME-ALLO-ILE-OH;BOC-N-ME-ALLO-ISOLEUCINE;BOC-MEALLOILE-OH;BOC-N-ALPHA-METHYL-L-ALLOISOLEUCINE;BOC-ALLO-MEILE-OH;N-ALPHA-T-BUTOXYCARBONYL-N-ALPHA-METHYL-L-ALLO-ISOLEUCINE;Boc-N-Me-allo-Ile-OH·CHA
• CAS NO: 136092-80-3
• Molecular Formula: C₁₂H₂₃NO₄
• Molecular Weight: 245.32
• Product Categories: amino acids
• Mol File: 136092-80-3.mol
• Article Data: 14

Chemical Properties

• Boiling Point: 338.2±21.0 °C(Predicted)
• Appearance: /
• Density: 1.053±0.06 g/cm3(Predicted)
• Storage Temp.: Store at RT.
• PKA: 4.05±0.22(Predicted)
• CAS DataBase Reference: BOC-N-ME-ALLO-ILE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-N-ME-ALLO-ILE-OH(136092-80-3)
• EPA Substance Registry System: BOC-N-ME-ALLO-ILE-OH(136092-80-3)

Safety Data

• Hazardous Substances Data: 136092-80-3(Hazardous Substances Data)

Usage

General Description

BOC-N-ME-ALLO-ILE-OH is a chemical compound, also known as N-Methyl-L-allo-isoleucine tert-butyl ester. It belongs to the category of organic compounds known as L-alpha-amino acids, which are proteinogenic amino acids that contain a carboxylic acid group (COOH) and an amine group (NH2). BOC-N-ME-ALLO-ILE-OH possesses protective groups like BOC (tert-butyloxycarbonyl), known for protecting an amine group in a molecule and commonly used in peptide synthesis. It is also to be noted that this specific chemical compound has been less studied compared to other amino acids, therefore, less is known about its properties or applications.

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 73-32-5 L-isoleucine 
• 13139-16-7 N-tert-butyloxy-isoleucine 
• 74-88-4 methyl iodide 
• 1509-34-8 D-allo-isoleucine 
• 58632-95-4 2-(tert-Butoxycarbonyloxyimino)-2-phenylacetonitrile 
• 13139-16-7 Boc-L-aIle-OH 
• 73-32-5 L-isoleucine 
• 13139-16-7 N-(tert-butyloxycarbonyl)-L-isoleucine 
• 77-78-1 dimethyl sulfate 

Downstream Products

• 73-32-5 L-isoleucine 
• 110417-88-4 dolastatin 10 

Relevant articles and documents

Highly N-methylated linear peptides produced by an atypical sponge-derived Acremonium sp.

RHM1 (1) and RHM2 (2) are highly N-methylated linear octapeptides produced by an atypical strain of Acremonium sp., cultured from a marine sponge collected in Papua New Guinea. The known peptaibiotic efrapeptin G (3) was also isolated from this fungus. The planar structures of 1 and 2 were assigned based on 1D- and 2D-NMR experiments and fragmentation patterns from ESIMS. The absolute configuration of 1 was determined via Marfey's method; the absolute configuration of 2 is proposed to be identical. Efrapeptin G (3) displayed potent cytotoxicity against murine cancer cell lines, while RHM1 (1) and RHM2 (2) showed weak cytotoxicity against murine cancer cell lines; efrapeptin G (3) and RHM1 (1) also demonstrated antibacterial activity.

Design, Synthesis, and Conformation-Activity Study of Unnatural Bridged Bicyclic Depsipeptides as Highly Potent Hypoxia Inducible Factor-1 Inhibitors and Antitumor Agents

By carrying out structural modifications based on the bicyclic peptide structure of echinomycin, we successfully synthesized various powerful antitumor derivatives. The ring conformation in the obtained compounds was restricted by cross-linking with an unnatural bond. The prepared derivatives were demonstrated to strongly suppress the hypoxia inducible factor (HIF)-1 transcriptional activation and hypoxia induction of HIF-1 protein expression. Particularly, alkene-bridged derivative 12 exhibited remarkably potent cytotoxicity (IC50 = 0.22 nM on the MCF-7 cell line) and HIF-1 inhibition (IC50 = 0.09 nM), which considerably exceeded those of echinomycin. Conformational analyses and molecular modeling studies revealed that the biological activities were enhanced following restriction of the conformation by cross-linking through a metabolically stable and rigid bridge bond. In addition, we proposed a new globular conformation stabilized by intramolecular πstacking that can contribute to the biological effects of bicyclic depsipeptides. The developments presented in the current study serve as a useful guide to expand the chemical space of peptides in drug discovery.

Total synthesis of modified pentapeptide, caldoramide

Total synthesis of modified pentapeptide, caldoramide, a cytotoxic linear pentapeptide from the marine cyanobacterium Caldora penicillate is described. Notable features of the route include the efficient preparation of three key fragments and final assemb

Design, synthesis, and in vitro antiplasmodial activity of 4-aminoquinolines containing modified amino acid conjugates

Abstract: A new series of side chain-modified 4-aminoquinolines were synthesized and screened for in vitro antiplasmodial activity against both chloroquine-sensitive (3D7) and chloroquine-resistant (K1) strains of Plasmodium falciparum. Among the series, compounds 30 and 31 showed significant inhibition of parasite growth against K1 strain of P. falciparum with IC50 values 0.28 and 0.31?μM, respectively, whereas compounds 34, 35, and 38 exhibited superior activity against K1 strain with IC50 values 0.18, 0.22, and 0.17?μM, respectively, as compared to 0.255?μM for chloroquine (CQ). All the compounds displayed good resistance factor between 1.54 and >34.48 as against 51.0 for CQ. All these analogues were found to form strong complex with hematin and inhibited the β-hematin formation in vitro, suggesting that this class of compounds act on a heme polymerization target. Overall results suggest that present series of compounds appear to be promising for further lead optimization to obtain compounds active against drug-resistant parasites. Graphical Abstract: [Figure not available: see fulltext.]