16937-99-8

Usage

Uses

Used in Pharmaceutical Industry:
BOC-D-Leucine monohydrate is used as an analgesic agent for its ability to cause analgesia in humans. It is also used as an inhibitor in bacterial cell cultures due to its inhibitory activity.
Used in Chemical Synthesis:
BOC-D-Leucine monohydrate is used as a protected amino acid in the synthesis of peptides and other organic compounds, where the N-Boc group can be selectively removed to reveal the free D-Leucine.
Used in Research and Development:
BOC-D-Leucine monohydrate is used as a research compound for studying the properties and applications of D-Leucine and its derivatives, as well as for investigating the mechanisms of auto-inhibition in lactic streptococci.

InChI:InChI=1/C11H21NO4.H2O/c1-7(2)6-8(9(13)14)12-10(15)16-11(3,4)5;/h7-8H,6H2,1-5H3,(H,12,15)(H,13,14);1H2/t8-;/m1./s1

Upstream product

• 1070-19-5 N-(tert-butyloxycarbonyl) azide 
• 328-38-1 (R)-leucine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 129568-83-8 (2R,2'R)-N-(2'-amino-4'-methylpentanoyl)bornane-10,2-sultam 
• 19792-08-6 p-nitrophenyl-N-(t-butoxycarbonyl)-D-leucinate 
• 41840-28-2 S-tert-butoxycarbonyl-4,6-dimethyl-2-mercaptopyrimidine 
• 54594-06-8 D-allylglycine 
• 106930-51-2 tert-butyl [(2R)-1-hydroxy-4-methylpentan-2-yl]carbamate 
• 69805-63-6 methyl 2-((tert-butoxycarbonyl)amino)-4-methylpentanoate 
• 73371-96-7 2-<<(tert-butoxycarbonyl)oxy>imino>-2-phenylacetonitrile 
• 126645-26-9 (S)-methyl 2-((tert-butoxycarbonyl)amino)-3-((tert-butyldimethylsilyl)oxy)propanoate 
• 38136-29-7 4-methylvaleroyl chloride 
• 129505-08-4 (2R,2'R)-N-<2'-(hydroxyamino)-4'-methylpentanoyl>bornane-10,2-sultam 
• 756498-96-1 ethyl N-tert-butyloxycarbonyl-2-amino-4-methyl-pentanoate 

Downstream Products

• 60654-42-4 Boc-D-Leu-NH-NH-Z 
• 116300-00-6 1-diazo-3(R)-<<(1,1-dimethylethoxy)carbonyl>amino>-5-methyl-2-hexanone 
• 83160-12-7 N^α-Tos-D-Lys-Gly-Phe-D-Leu-OH 
• 78834-53-4 BOC-D-Leu-L-Val-pNA 
• 140834-91-9 Boc-D-Leu-Phe-OBzl 
• 137022-74-3 Boc-D-Leu-Gly-NHOBzl 
• 137029-92-6 [(R)-1-((S)-1-Benzyl-2-oxo-2-piperidin-1-yl-ethylcarbamoyl)-3-methyl-butyl]-carbamic acid tert-butyl ester 
• 137005-62-0 {(R)-1-[(S)-1-Benzyl-2-oxo-2-(4-phenyl-piperidin-1-yl)-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid tert-butyl ester 
• 137005-63-1 {(R)-1-[(S)-1-Benzyl-2-oxo-2-(4-phenyl-piperazin-1-yl)-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid tert-butyl ester 
• 137005-64-2 ((R)-1-{(S)-2-[4-(4-Acetyl-phenyl)-piperazin-1-yl]-1-benzyl-2-oxo-ethylcarbamoyl}-3-methyl-butyl)-carbamic acid tert-butyl ester 
• 137005-65-3 {(R)-1-[(S)-2-(4-Benzo[1,3]dioxol-5-ylmethyl-piperazin-1-yl)-1-benzyl-2-oxo-ethylcarbamoyl]-3-methyl-butyl}-carbamic acid tert-butyl ester 
• 77302-94-4 (S)-2-{(S)-4-Benzyloxycarbonyl-2-[(S)-4-benzyloxycarbonyl-2-((R)-2-tert-butoxycarbonylamino-4-methyl-pentanoylamino)-butyrylamino]-butyrylamino}-4-methyl-pentanoic acid methyl ester 
• 77302-93-3 (R)-2-{(S)-4-Benzyloxycarbonyl-2-[(S)-4-benzyloxycarbonyl-2-((R)-2-tert-butoxycarbonylamino-4-methyl-pentanoylamino)-butyrylamino]-butyrylamino}-4-methyl-pentanoic acid methyl ester 
• 78834-52-3 BOC-D-Leu-D-Val-pNA 

Relevant academic research and scientific papers

Preparation method of N-trimethyl silicon ethoxycarbonyl-N-methyl-L/D-leucine

The invention relates to a preparation method of N-(trimethylsilyl) ethoxycarbonyl group-N-methyl-L/D-leucine. The preparation method comprises the following steps: adding N-methyl-L/D-leucine hydrochloride, a trimethylsilylethoxycarbonyl protecting group reagent and alkali into a mixed solution of a polar solvent and water, and carrying out a reaction, so as to obtain the N-trimethylsilylethoxycarbonyl-N-methyl-L/D-leucine. According to the preparation method, the N-trimethyl silicon ethoxycarbonyl-N-methyl-L/D-leucine with high chiral purity, high chemical purity and high yield can be obtained, the chiral purity and the chemical purity can reach 99% or above, the yield can reach 60% or above, and the preparation method is simple in process, mild in condition and suitable for being applied to large-scale industrial production.

D-amino acid position influences the anticancer activity of galaxamide analogs: An apoptotic mechanism study

Galaxamide, an extract from Galaxaura filamentosa, is a cyclic pentapeptide containing five L-leucines. Due to the particular cyclic structure and the excellent anticancer activity, synthesis of Galaxamide and its analogs and their subsequent bio-applications have attracted great attention. In the present work, we synthesized six Galaxamide analogs by replacing one of the L-leucines with phenylalanine and varying the D-amino acid position. The anticancer effect of the synthesized Galaxamide analogs was tested against four in vitro human cancer cell lines, human hepatocellular cells (HepG2), human breast cancer cell (MCF-7), human breast adenocarcinoma cells (MDA-MB-435) and a human cervical carcinoma cell line (Hela). Results showed that Galaxamide analogs with differentD-amino acid positions displayed distinct anticancer potential. The Galaxamide analog containing D-amino acid at position 5 (Analog-6) presented the strongest anticancer activity. The mechanism study revealed that Analog-6 could cause the early apoptosis of HepG2 cells by inhibiting their growth in the sub-G1 stage of the cell cycle and induce the chromatin condensation and fragmentation, which can be seen as 68% of HepG2 cells inhibited in the sub-G1 stage. Moreover, a mitochondria-mediated pathway was found to be involved in the apoptotic process of Analog-6 on HepG2 cells.

Optical resolution of N-(t-butoxycarbonyl)leucine through mixed ligand complex formation with (R)-N-(2-pyridylmethyl)pipecolatocopper(II)

A copper(II) complex of (R)-N-(2-pyridylmethyl)pipecolate (pmpi) was prepared, and its structure was revealed by X-ray crystal structure analysis. Mixed ligand complexes were then prepared from this complex and (R)- and (S)-N-(t-butoxycarbonyl)leucinate (BocLeu). The (R)-BocLeu complex is less soluble in aqueous acetonitrile and more soluble in acetone than the (S)-BocLeu complex, and the reason was discussed on the basis of their structures. Recrystallization of the reaction mixture consisting of Cu(II) ion, pmpi, and (RS)-BocLeu from aqueous acetonitrile gave the (R)-BocLeu complex and that from acetone gave the (S)-BocLeu complex.

PROLINAMIDE DERIVATIVE AS THROMBIN INHIBITOR, PREPARATION METHOD AND APPLICATION THEREOF

Provided are a compound of formula (I), pharmaceutically acceptable salts thereof, preparation methods and applications thereof for inhibiting thrombin, and applications in the treatment and prevention of thrombin-mediated and thrombin-related diseases.

PROLINAMIADE DERIVATIVES AS THROMBIN INHIBITOR, PREPRARATION METHOD AND APPLICATION THEREOF

Provided are a compound of formula (I), pharmaceutically acceptable salts thereof, preparation methods and applications thereof for inhibiting thrombin, and applications in the treatment and prevention of thrombin-mediated and thrombin-related diseases.

Synthetic Studies of Tamandarin B Side Chain Analogues

The syntheses of three tamandarin B analogues are described. The goal of these studies was to prepare material to determine their relative therapeutic index and to gain an oversight as to their potential for clinical applications.

Synthetic studies on chlorofusin: Synthesis of the cyclic peptide portion

The cyclic peptide portion of chlorofusin was synthesized by condensation of the five segments, d-Ada-OTMSE, Boc-l.-Orn(Cbz), Boc-l-Thr-l-Ala, l-Asn(Tr)-d-Asn(Tr)-d-Leu-OTMSE, and Boc-l-Thr-d-Leu, followed by cyclization at the amide bond between d-Ada an

Synthesis and biological evaluation of chiral α-aminoanilides with central antinociceptive activity

Tocainide and related optically active chiral α-aminoanilides were synthesized and tested in vivo via the hot plate test to evaluate their central analgesic action. The aims of the study were to verify if a) the increase in lipophilicity, obtained by the introduction of an alkyl group on the steric center (3f-i), and the replacement of the C=O group with the C=S (10) group as well as the introduction of a methyl or ethyl group on the amidic nitrogen atom (8a-c) would produce an increase in central analgesic efficacy with respect to Tocainide; b) the 2,6-xylidide moiety is crucial for high analgesic activity (3b-e); c) the hydrogen atom bonded to the amidic nitrogen moiety is an essential pharmacophoric element for analgesic activity. Among all the synthesized compounds, 3f showed antinociceptive properties with a good enantioselective index.

Enzymatic approach to both enantiomers of N-Boc hydrophobic amino acids

Protease catalysed hydrolysis of N-Boc-amino acid esters allows us to obtain N-Boc l-acids and d-esters of amino butanoic acid, nor-leucine, nor-valine, leucine and t-leucine in excellent ee. The reaction occurs in short reaction times and high concentrations. When a biphasic system (buffer-MTBE) is employed, a strong solvent effect is observed. This method could be of significance for the preparation of d-t-leucine, for which a practical method is currently unavailable.

The role of the disulfide bond in amyloid-like fibrillogenesis in a model peptide system

Three terminally protected short peptides Bis[Boc-D-Leu(1)-Cys(2)-OMe] 1, Bis[Boc-Leu(1)-Cys(2)-OMe] 2 and Bis[Boc-Val(1)-Cys(2)-OMe] 3 exhibit amyloid-like fibrillar morphology. Single crystal X-ray diffraction analysis of peptide 1 clearly demonstrates that it adopts an overall extended backbone molecular conformation that self-assembles to form an intermolecular hydrogen-bonded antiparallel supramolecular β-sheet structure in crystals. Scanning electron microscopic (SEM) images, transmission electron microscopic (TEM) images and Congo red binding studies vividly demonstrate the amyloid-like fibril formation of peptides 1, 2 and 3. However, after reduction of the disulfide bridge of peptides 1, 2 and 3, three newly generated peptides Boc-D-Leu(1)-Cys(2)-OMe 4, Boc-Leu(1)-Cys(2)-OMe 5 and Boc-Val(1)-Cys(2)-OMe 6 are formed and all of them failed to form any kind of fibril under the same conditions, indicating the important role of the disulfide bond in amyloid-like fibrillogenesis in a peptide model system. The Royal Society of Chemistry 2005.