55677-48-0

Basic information

• Product Name: BOC-PHE-ALA-OH
• Synonyms: BOC-L-PHENYLALANYL ALANINE;BOC-PHE-ALA-OH;l-Alanine, N-[N-[(1,1-dimethylethoxy)carbonyl]-l-phenylalanyl]-;t-butyloxycarbonylphenylalanylalanine;Boc-L-Phe-L-Ala-OH
• CAS NO: 55677-48-0
• Molecular Formula: C₁₇H₂₄N₂O₅
• Molecular Weight: 336.38
• Mol File: 55677-48-0.mol

Chemical Properties

• Melting Point: 90-93 °C(Solv: chloroform (67-66-3); hexane (110-54-3))
• Boiling Point: 587.8°Cat760mmHg
• Flash Point: 309.3°C
• Appearance: /
• Density: 1.182g/cm³
• Vapor Pressure: 1.17E-14mmHg at 25°C
• Refractive Index: 1.53
• Storage Temp.: Store at 0°C
• PKA: 3.51±0.10(Predicted)
• CAS DataBase Reference: BOC-PHE-ALA-OH(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-PHE-ALA-OH(55677-48-0)
• EPA Substance Registry System: BOC-PHE-ALA-OH(55677-48-0)

Safety Data

• Hazardous Substances Data: 55677-48-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
BOC-PHE-ALA-OH is used as a building block for the synthesis of larger peptides and proteins, facilitating the development of novel pharmaceutical compounds with specific therapeutic properties.
Used in Biochemical Studies:
BOC-PHE-ALA-OH is used as a valuable tool in studying the structure and function of biological molecules, contributing to a better understanding of their mechanisms and potential applications in medicine.
Used in Drug Production:
BOC-PHE-ALA-OH is used as an important intermediate in the production of pharmaceutical drugs, enabling the creation of new and effective medications for various diseases and conditions.

InChI:InChI=1/C17H24N2O5/c1-11(15(21)22)18-14(20)13(10-12-8-6-5-7-9-12)19-16(23)24-17(2,3)4/h5-9,11,13H,10H2,1-4H3,(H,18,20)(H,19,23)(H,21,22)/t11-,13-/m0/s1

Upstream product

• 56-41-7 L-alanin 
• 514214-66-5 (S)-tert-butyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 15136-29-5 (S)-methyl 2-((S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)propanoate 
• 24424-99-5 di-tert-butyl dicarbonate 
• 3918-87-4 N-L-phenylalanyl-L-alanine 
• 67729-36-6 Boc-Phe-O-COO-isoBu 
• 3674-06-4 Boc-Phe-ONSu 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 885623-82-5 (S)-2-((S)-2-tert-Butoxycarbonylamino-3-phenyl-propionylamino)-propionic acid 2-[(4,4,5,5,6,6,7,7,8,8,9,9,10,10,11,11,11-heptadecafluoro-undecyl)-dimethyl-silanyl]-ethyl ester 
• 98228-99-0 BOC-L-Phe-L-Ala-CAM 
• 133565-23-8 Alanine benzyltrimethylammonium salt 

Downstream Products

• 70396-33-7 Boc-L-Phe-L-Ala-L-Leu-OMe 
• 1017573-18-0 t-butyloxycarbonyl-L-phenylalanyl-L-alanyl-L-phenylalanyl-L-proline methyl ester 
• 110205-82-8 (2R,3S)-3-<(Boc-L-phenylalanylalanyl)amino>-2-hydroxy-4-cyclohexyl-1-(isopropylthio)butane 
• 110613-40-6 ((S)-1-{(S)-1-[(S)-1-Cyclohexylmethyl-4-(2-dimethylamino-ethylcarbamoyl)-2-hydroxy-pent-4-enylcarbamoyl]-ethylcarbamoyl}-2-phenyl-ethyl)-carbamic acid tert-butyl ester 

Relevant articles and documents

Tripeptide based super-organogelators: Structure and function

A novel series of tripeptide-based low molecular weight super-organogelators were synthesized and characterized. Four tripeptides with diverse steric crowding at the central amino acid residue were studied. From this series, only sterically less hindered

Α-BORYL ISOCYANIDES, BOROPEPTIDES AND BORON HETEROCYCLES

This application pertains to α-boryl isocyanates, wherein the boronate moiety is in the form of an N-methyliminodiacetic acid (MIDA) boronate of the Formula (2) and the utility of said compounds in the synthesis of the borylamide motif (Β-C-Namide) in the scaffold of biologically-active boropeptides, such as bortezomib, in the enablement of heterocycle synthesis, and in multi-component reactions (MCRs), such as the Ugi and Passerini processes.

α-boryl isocyanides enable facile preparation of bioactive boropeptides

Entry to bioactive boropeptides: MIDA-containing α-boryl isocyanides are isolable molecules which allow one-step access to boroalkyl-functionalized heterocycles as well as biologically active boropeptides through a multicomponent approach. Among these derivatives are 6-boromorpholinones, novel borocycles with nanomolar IC50 values for 20S proteasome inhibition. MIDA=N-methyliminodiacetyl. Copyright

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.

Epimerization-free C-terminal peptide activation

Smooth operation: C-terminal peptide activation with full stereointegrity was accomplished using a copper(II)-mediated coupling reaction of carboxylic acids with arylboroxines (see scheme, NCL = native chemical ligation, Boc = tert-butoxycarbonyl). This method allows epimerization-free activation and ligation of peptides with racemization-prone phenylglycine at the C terminus.

Evaluation of α,β-unsaturated ketone-based probes for papain-family cysteine proteases

The field of activity-based proteomics makes use of small molecule active site probes to monitor distinct subsets of enzymatic proteins. While a number of reactive functional groups have been applied to activity-based probes (ABPs) that target diverse families of proteases, there remains a continual need for further evaluation of new probe scaffolds and reactive functional groups for use in ABPs. In this study we evaluate the utility of the, α,β-unsaturated ketone reactive group for use in ABPs targeting the papain-family of cysteine proteases. We find that this reactive group shows highly selective labeling of cysteine cathepsins in both intact cells and total cell extracts. We observed a variable degree of background labeling that depended on the type of tag and linker used in the probe synthesis. The relative ease of synthesis of this class of compounds provides the potential for further derivatization to generate new families of cysteine protease ABPs with unique specificity and labeling properties.

Synthesis and pharmacological investigation of segetalin C as a novel antifungal and cytotoxic agent

In present study, a natural phenylalanine-rich cycloheptapeptide segetalin C (compound VIII) was synthesized by coupling and cyclization of peptide units Boc-gly-L-leu-L-his-OH and L-Phe-L-ala-L-phe-L-pro-OMe and examined for different bioactivities. The

Fluorous (trimethylsilyl)ethanol: A new reagent for carboxylic acid tagging and protection in peptide synthesis

Starting with a fluorous analogue of 2-(trimethylsilyl)ethanol, we have designed an easy method for preparing a new fluorous tag (FTMSE) for the protection of carboxylic acids. Because mild conditions are employed in the tag cleavage (TBAF in the presence of 4 A molecular sieves, which prevent racemization), this tag can be advantageously used in the synthesis of peptides and modified peptides, as we have demonstrated with several examples, including the fluorous synthesis of short α- and β-peptides as well as of modified fluorinated retropeptides.

Highly diastereoselective peptide chain extensions of unprotected amino acids with N-(Z-α-aminoacyl)benzotriazoles

Coupling an unprotected amino acid or dipeptide in partially aqueous solution with a readily available N-(Z-α-amino-acyl)benzotriazole or N-(Z-α-aminopetidoyl)benzotriazole affords N-terminal-protected di-, tri-, and tetrapeptides in yields of 85-98% (average 95% for 2a-i, 93% for 4a-f and 4a′, 86% for 5a-b) with minimal epimerization.

Comparative lipase-catalyzed hydrolysis of ethylene glycol derived esters. The 2-methoxyethyl ester as a protective group in peptide and glycopeptide synthesis

Comparison of the lipase-catalyzed cleavage of polar esters derived from ethylene glycol proved 2-methoxyethyl (ME) esters most favorable protecting groups for the carboxylic function of peptides and glycopeptides. They combine high substrate acceptance and iligh yields of hydrolysis with favorable physicochemical properties and advantageous solubility. The application of this polar ester as protecting group was extended to N-glycosylated amino acids and N-glycopeptides. The selective removal of ME esters by lipases was achieved under mild conditions (pH 7.0 and 37°C), leaving all other linkages including peptide bonds and other ester protecting groups unaffected.