15136-29-5

Basic information

• Product Name: BOC-PHE-ALA-OME
• Synonyms: BOC-L-PHENYLALANYL ALANYL METHYL ESTER;BOC-PHE-ALA-OME;Boc-L-Phe-L-Ala-OMe;N-Boc-L-Phe-L-Ala-OMe;(S)-methyl 2-((S)-2-(tert-butoxycarbonylamino)-3-phenylpropanamido)propanoate;REF DUPL: Boc-Phe-Ala-OMe;(S)-methyl 2-((S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)propanoate(WXG03307)
• CAS NO: 15136-29-5
• Molecular Formula: C₁₈H₂₆N₂O₅
• Molecular Weight: 350.41
• Mol File: 15136-29-5.mol

Chemical Properties

• Melting Point: 103-104 °C(Solv: chloroform (67-66-3); ligroine (8032-32-4))
• Boiling Point: 526 °C at 760 mmHg
• Flash Point: 271.9 °C
• Appearance: /
• Density: 1.13 g/cm³
• Vapor Pressure: 3.72E-11mmHg at 25°C
• Refractive Index: 1.51
• Storage Temp.: Store at 0°C
• PKA: 11.29±0.46(Predicted)
• CAS DataBase Reference: BOC-PHE-ALA-OME(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-PHE-ALA-OME(15136-29-5)
• EPA Substance Registry System: BOC-PHE-ALA-OME(15136-29-5)

Safety Data

• Hazardous Substances Data: 15136-29-5(Hazardous Substances Data)

Usage

Uses

Used in Biochemistry Research:
BOC-PHE-ALA-OME is used as a building block for the synthesis of peptides and proteins, contributing to the development of novel bioactive molecules and therapeutic agents. Its N-protected structure ensures the molecule's stability during the synthesis process, allowing for precise control over the peptide assembly.
Used in Pharmaceutical Development:
In the pharmaceutical industry, BOC-PHE-ALA-OME is employed as a key intermediate in the synthesis of potential drug candidates. Its protected amino acid structure enables the creation of complex peptide-based drugs with specific biological activities, such as enzyme inhibitors or receptor agonists/antagonists.
Used in Academic Research:
BOC-PHE-ALA-OME serves as an essential tool in academic research, where it is used to study the structure-function relationships of peptides and proteins. Its protected nature allows researchers to investigate the effects of amino acid modifications on protein folding, stability, and biological activity, thereby advancing our understanding of protein biology and its implications in health and disease.

InChI:InChI=1/C18H26N2O5/c1-12(16(22)24-5)19-15(21)14(11-13-9-7-6-8-10-13)20-17(23)25-18(2,3)4/h6-10,12,14H,11H2,1-5H3,(H,19,21)(H,20,23)

Upstream product

• 186581-53-3 diazomethane 
• 55677-48-0 N-tert-butyloxycarbonyl-L-phenylalanyl-L-alanine 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 2491-20-5 L-alanine methyl ester hydrochloride 
• 591-50-4 iodobenzene 
• 170454-73-6 (S)-2-((R)-2-tert-Butoxycarbonylamino-3-iodo-propionylamino)-propionic acid methyl ester 
• 10065-72-2 L-Alanine methyl ester 
• 146346-88-5 methyl 2-(((9H-fluoren-9-yl)methoxy)carbonyl)aminopropanoate 
• 50903-54-3 N-[(1,1-dimethylethoxy)carbonyl]-L-phenylalanine pentafluorophenyl ester 
• 3674-06-4 Boc-Phe-ONSu 
• 98228-99-0 BOC-L-Phe-L-Ala-CAM 
• 142955-51-9 N-butoxycarbonyl-L-phenylalanine anhydride 
• 6003-05-0 L-alanine hydrochloride 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 

Downstream Products

• 78605-47-7 Boc-Phe-Ala-OEt 
• 3338-40-7 L-phenylalanine-L-alanine methyl ester hydrochloride 
• 136497-26-2 Boc-Phe-Ala-OCH₂CH=CH₂ 
• 136497-25-1 Boc-Phe-Ala-OCHMe₂ 
• 81109-94-6 methyl (2S)‐2‐[(2S)‐2‐amino‐3‐phenylpropanamido]propanoate trifluoroacetate 
• 136497-27-3 Boc-Phe-Ala-OCMe₃ 
• 80870-39-9 D-phenylalanine-L-alanine methylester 
• 94776-26-8 -L-phenylalanyl-L-alanine mehtyl ester 
• 94776-33-7 1-N--β-D-glucopyranosylamine 
• 82155-29-1 2-acetamido-1-N--2-deoxy-β-D-glucopyranosylamine 
• 82155-33-7 1-N--4-O-(β-D-glucopyranosyl)-β-D-glucopyranosylamine 
• 55677-48-0 N-tert-butyloxycarbonyl-L-phenylalanyl-L-alanine 
• 139341-11-0 C₁₈H₂₆N₂O₄S 
• 1332650-74-4 tert-butyl (S)-1-(4-((S)-1-(methoxycarbonyl)ethyl)-5-((S)-1-Boc-amino-2-phenylethyl)-4H-1,2,4-triazol-3-yl)-2-phenylethylcarbamate 

Relevant articles and documents

Sequential One-Pot Synthesis of Dipeptides through the Transient Formation of CDI-N-Protected α-Aminoesters

The synthesis of dipeptides through a sequential one-pot procedure from commercially available protected amino acids is described. The transformation relies on the use of in situ generated transiently CDI-protected α-amino esters (CDI, e.g. N,N′-carbonyldiimidazole). In addition of being a highly atom-economical process, the couplings take place under very mild and neutral conditions without adding a base to the reaction medium. This protocol provides a concise and less costly route to dipeptide derivatives (12 examples, up to 87% yield) and is compatible with commonly used N-urethane protecting groups. Moreover, no epimerization was detected even when sensitive Boc-Cys(Bn)?OH was used. (Figure presented.).

Controlling Syneresis of Hydrogels Using Organic Salts

Supramolecular hydrogels can spontaneously undergo syneresis through fibre–fibre interactions and expel significant amounts of water upon aging. In this process, the hydrophobicity of fibres which regulates the 3D-rearrangement of the self-assembled struc

Optimization and anti-cancer properties of fluoromethylketones as covalent inhibitors for ubiquitin C-terminal hydrolase L1

The deubiquitinating enzyme (DUB) UCHL1 is implicated in various disease states including neurodegenerative disease and cancer. However, there is a lack of quality probe molecules to gain a better understanding on UCHL1 biology. To this end a study was carried out to fully characterize and optimize the irreversible covalent UCHL1 inhibitor VAEFMK. Structure-activity relationship studies identified modifications to improve activity versus the target and a full cellular characterization was carried out for the first time with this scaffold. The studies produced a new inhibitor, 34, with an IC50 value of 7.7 μM against UCHL1 and no observable activity versus the closest related DUB UCHL3. The molecule was also capable of selectively inhibiting UCHL1 in cells and did not demonstrate any discernible off-target toxicity. Finally, the molecule was used for initial probe studies to assess the role of UCHL1 role in proliferation of myeloma cells and migration behavior in small cell lung cancer cells making 34 a new tool to be used in the biological evaluation of UCHL1.

Effect of Stereochemistry on Chirality and Gelation Properties of Supramolecular Self-Assemblies

Although chiral nanostructures have been fabricated at various structural levels, the transfer and amplification of chirality from molecules to supramolecular self-assemblies are still puzzling, especially for heterochiral molecules. Herein, four series o

Cobalt-Catalyzed C(sp2)-H Carbonylation of Amino Acids Using Picolinamide as a Traceless Directing Group

Herein we report an efficient protocol for the C(sp2)-H carbonylation of amino acid derivatives based on an inexpensive cobalt(II) salt catalyst. Carbonylation was accomplished using picolinamide as a traceless directing group, CO (1 atm) as the carbonyl

Chiral Overpass Induction in Dynamic Helical Polymers Bearing Pendant Groups with Two Chiral Centers

The dynamic behavior of helical polymers bearing pendant groups with two chiral centers was studied. Controlled conformational changes at the chiral units placed either closer to or further away from the main chain promote different helical structures. Al

Peptide Bond Formation via Nα-Protected Diacyldiselenides

Abstract: A simple, straightforward, for the peptide bond formation employing corresponding carboxylic acids and amines derived from amino acids via Nα-protected diacyldiselenide is delineated. The key step of the synthesis is the in situ gener

Substrate-directed lewis-acid catalysis for peptide synthesis

A Lewis-acid-catalyzed method for the substrate-directed formation of peptide bonds has been developed, and this powerful approach is utilized for the new "remote" activation of carboxyl groups under solvent-free conditions. The presented method has the following advantages: (1) the high-yielding peptide synthesis uses a tantalum catalyst for any amino acids; (2) the reaction proceeds without any racemization; (3) the new substrate-directed chemical ligation using the titanium catalyst is applicable to convergent peptide synthesis. These advantages overcome some of the unresolved problems in classical peptide synthesis.

In vitro and in silico determination of glutaminyl cyclase inhibitors

Alzheimer's disease (AD) is the most common form of neurodegenerative disease currently. It is widely accepted that AD is characterized by the self-assembly of amyloid beta (Aβ) peptides. The human glutaminyl cyclase (hQC) enzyme is characterized by assoc

REDOX DEHYDRATION COUPLING CATALYSTS AND METHODS RELATED THERETO

This disclosure relates to synthetic coupling methods using catalytic molecules. In certain embodiments, the catalytic molecules comprise heterocyclic thiolamide, S-acylthiosalicylamide, disulfide, selenium containing heterocycle, diselenide compound, ditelluride compound or tellurium containing heterocycle. Catalytic molecules disclosed herein are useful as catalysts in the transformation of hydroxy group containing compounds to amides, esters, ketones, and other carbon to heteroatom or carbon to carbon transformations.