5874-73-7

Usage

Uses

Used in Pharmaceutical Industry:
Tert-butyloxycarbonyl-leucylphenylalanine methyl ester is used as a protective group in peptide synthesis for the development of bioactive peptides and pharmaceuticals. Its ability to shield the amine group and provide protection at the C-terminus allows for precise and controlled synthesis, which is crucial for the production of effective and stable peptide-based drugs.
Used in Bioactive Peptide Production:
In the field of bioactive peptide production, tert-butyloxycarbonyl-leucylphenylalanine methyl ester is used as a key component in the synthesis process. Its protective properties ensure that the desired peptide sequence is accurately formed without unwanted side reactions, resulting in high-quality bioactive peptides with potential applications in various industries, such as food, cosmetics, and healthcare.
Used in Research and Development:
Tert-butyloxycarbonyl-leucylphenylalanine methyl ester is also utilized in research and development settings for the study of peptide synthesis and the development of new synthetic methods. Its protective capabilities allow researchers to explore novel approaches to peptide synthesis, potentially leading to more efficient and effective production techniques.

InChI:InChI=1/C21H32N2O5/c1-14(2)12-16(23-20(26)28-21(3,4)5)18(24)22-17(19(25)27-6)13-15-10-8-7-9-11-15/h7-11,14,16-17H,12-13H2,1-6H3,(H,22,24)(H,23,26)/t16-,17-/m0/s1

Upstream product

• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 140834-91-9 (S)-benzyl 2-((S)-2-(tert-butoxycarbonylamino)-4-methylpentanamido)-3-phenylpropanoate 
• 67436-23-1 phenylalanine methyl ester tosylate 
• 17349-27-8 NPS-Phe-OMe 
• 2688-22-4 Nps-L-Phe-OH 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 200937-21-9 N-tert-butoxycarbonyl-L-leucine monohydrate 
• 61-90-5 L-leucine 
• 24424-99-5 di-tert-butyl dicarbonate 
• 63-91-2 L-phenylalanine 
• 66866-44-2 Boc-Leu-O-COO-isoBu 

Downstream Products

• 75286-44-1 Boc-Leu-Phe-Leu-NH₂ 
• 145250-92-6 (S)-2-[(S)-2-((S)-2-tert-Butoxycarbonylamino-4-methyl-pentanoylamino)-3-phenyl-propionylamino]-4-methyl-pentanoic acid 
• 79259-41-9 Boc-Leu-Phe-Met-NH₂ 
• 859-45-0 N-trifluoroacetyl-leucylphenylalanine methylester 
• 1285537-76-9 Boc-Thia-Leu-Phe-OMe 
• 3063-05-6 Leu-Phe-OH 
• 1224467-09-7 N-phenyl-L-leucine-L-phenylalanine methyl ester 
• 1414493-21-2 tert-butyl (2S,3S,6S)-3-benzyl-2-(iodomethyl)-6-isobutyl-5-oxopiperazine-1-carboxylate 
• 1374225-27-0 C₅₅H₉₃N₉O₁₂ 
• 1365292-35-8 L-isoseryl-L-leucyl-L-phenylalanine methyl ester hydrochloride 
• 1371597-18-0 C₂₇H₄₃N₃O₆ 
• 1367281-41-1 C₁₈H₂₅BrN₂O₄ 
• 1367281-24-0 (Boc)2-[12]aneN₃-CH₂CO-Leu-Phe-OCH₃ 
• 26055-05-0 N-[N-(tert-butoxycarbonyl)-L-leucyl]-L-phenylalanine 

Relevant academic research and scientific papers

Preparation and biological evaluation of soluble tetrapeptide epoxyketone proteasome inhibitors

A series of novel tetrapeptidyl epoxyketone inhibitors of 20S proteasome was designed and synthesized. To fully understand the SAR, various groups at R1, R2, R3, R4 and R5 positions, including aromatic and aliphatic substituents were designed, synthesized and biologically assayed. Based on the enzymatic results, seven compounds were selected to evaluate their cellular activities and soluble compound 36 showed strong potency against human multiple myeloma (MM) cell lines. Microsomal stability results indicated that compound 36 was more stable in mice, rat and human microsomes than marketed carfilzomib. The in vivo activities of this compound were evaluated with the xenograft mice models of MM cell lines ARH77 and RPMI-8226 with luciferase expression and the T/C value of the two models were 49.5% and 37.6%, respectively. To evaluate the potential cardiovascular toxicity, inhibition of hERG ion channel in HEK293 cells by compound 36 and carfilzomib was carried out. The results indicated that 36 had no binding affinity for the hERG ion channel while carfilzomib could bind it with IC50 of 92.1 μM.

The role of N-terminal heterocycles in hydrogen bonding to α-chymotrypsin

A series of dipeptide aldehydes containing different N-terminal heterocycles was prepared and assayed in vitro against α-chymotrypsin to ascertain the importance of the heterocycle in maintaining a β-strand geometry while also providing a hydrogen bond do

Pd-Catalyzed Site-Selective C(sp2)-H Olefination and Alkynylation of Phenylalanine Residues in Peptides

Pd-catalyzed site-selective C(sp2)-H olefination and alkynylation of phenylalanine residues in peptides are described. The amino acids within the peptides are used as native bidentate directing groups to facilitate C-H functionalization. This p

Pd-catalyzed intramolecular C(sp2)-H amination of phenylalanine moieties in dipeptides: Synthesis of indoline-2-carboxylate-containing dipeptides

A palladium-catalyzed intramolecular C(sp2)-H amination of phenylalanine moieties in dipeptides is described. By this protocol, a series of indoline-2-carboxylate-containing dipeptides were synthesized from dipeptides. The N-protected amino aci

Target Validation and Identification of Novel Boronate Inhibitors of the Plasmodium falciparum Proteasome

The Plasmodium proteasome represents a potential antimalarial drug target for compounds with activity against multiple life cycle stages. We screened a library of human proteasome inhibitors (peptidyl boronic acids) and compared activities against purified P. falciparum and human 20S proteasomes. We chose four hits that potently inhibit parasite growth and show a range of selectivities for inhibition of the growth of P. falciparum compared with human cell lines. P. falciparum was selected for resistance in vitro to the clinically used proteasome inhibitor, bortezomib, and whole genome sequencing was applied to identify mutations in the proteasome β5 subunit. Active site profiling revealed inhibitor features that enable retention of potent activity against the bortezomib-resistant line. Substrate profiling reveals P. falciparum 20S proteasome active site preferences that will inform attempts to design more selective inhibitors. This work provides a starting point for the identification of antimalarial drug leads that selectively target the P. falciparum proteasome.

A dipeptide-based superhydrogel: Removal of toxic dyes and heavy metal ions from waste water

A short peptide-based molecule has been found to form a strong hydrogel at phosphate buffer solution of pH 7.46. The hydrogel has been characterized thoroughly using various techniques including field emission scanning electron microscopy (FE-SEM), wide angle powder X-ray diffraction (PXRD), and rheological analysis. It has been observed from FE-SEM images that entangled nanofiber network is responsible for gelation. Rheological investigation demonstrates that the self-assembly of this synthetic dipeptide results in the formation of mechanically strong hydrogel with storage modulus (G′) around 104 Pa. This gel has been used for removing both cationic and anionic toxic organic dyes (Brilliant Blue, Congo red, Malachite Green, Rhodamine B) and metal ions (Co2+ and Ni2+) from waste water. Moreover, only a small amount of the gelator is required (less than 1 mg/mL) for preparation of this superhydrogel and even this hydrogel can be reused three times for dye/metal ion absorption. This signifies the importance of the hydrogel towards waste water management.

Synthesis of Natural and Unnatural Cyclooligomeric Depsipeptides Enabled by Flow Chemistry

Flow chemistry has been successfully integrated into the synthesis of a series of cyclooligomeric depsipeptides of three different ring sizes including the natural products beauvericin (1 a), bassianolide (2 b) and enniatin C (1 b). A reliable flow chemistry protocol was established for the coupling and macrocyclisation to form challenging N-methylated amides. This flexible approach has allowed the rapid synthesis of both natural and unnatural depsipeptides in high yields, enabling further exploration of their promising biological activity. Harnessing technology: Flow chemistry has been successfully integrated into the synthesis of a series of cyclooligomeric depsipeptides of three different ring sizes including the natural products beauvericin (1 a), bassianolide (2 b) and enniatin C (1 b), resulting in increased overall yields, while decreasing the effort required for the researcher.

METHODS OF MAKING CARFILZOMIB AND INTERMEDIATES THEREOF

Racemization-free methods are disclosed for the synthesis of carfilzomib. Novel intermediates and methods of making carfilzomib employing fragment condensation using the novel intermediates are disclosed. Amorphous carfilzomib and methods of making same are disclosed.

PROCESS FOR THE PREPARATION OF (2S)-N-((S)-1-((S)-4-METHYL-1-((R)-2-METHYL OXIRAN-2-YL)-1-OXOPENTAN-2-YLCARBAMOYL)-2-PHENYLETHYL)-2-((S)-2-(2-MORPHOLINO ACETAMIDO)-4-PHENYLBUTANAMIDO)-4-METHYLPENTANAMIDE

The present invention relates to process for the preparation of (2S)-N-((S)-l -((S)-4-methyl-1 -((R)-2-methyloxiran-2-yl)-1-oxopentan-2-ylcarbamoyl)-2-phenylethyl)-2-((S)-2-(2-morpholinoacetamido)-4-phenylbutanamido)-4 -methylpentanamide represented by the following structural formula-1.

Towards the first total synthesis and anticancer screening of polycarponin C: A cyclic octapeptide

The present study describes designing, synthesis and anticancer screening of a proline rich cyclic octapeptide polycarponin C, by solution phase synthesis. The synthesis was carried out by coupling a tetrapeptide Boc-Pro-Thr-Leu-Pro-OH with another tetrap