34290-59-0

Basic information

• Product Name: BOC-PHE-SER-OME
• Synonyms: BOC-PHE-SER-OME
• CAS NO: 34290-59-0
• Molecular Formula: C₁₈H₂₆N₂O₆
• Molecular Weight: 366.41
• Mol File: 34290-59-0.mol

Chemical Properties

• Melting Point: 88-89 °C
• Boiling Point: 598.3 °C at 760 mmHg
• Flash Point: 315.7 °C
• Appearance: /
• Density: 1.192 g/cm³
• Vapor Pressure: 3.65E-15mmHg at 25°C
• Refractive Index: 1.525
• PKA: 11.27±0.46(Predicted)
• CAS DataBase Reference: BOC-PHE-SER-OME(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-PHE-SER-OME(34290-59-0)
• EPA Substance Registry System: BOC-PHE-SER-OME(34290-59-0)

Safety Data

• Hazardous Substances Data: 34290-59-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Boc-Phe-Ser-Ome is used as a building block in the synthesis of peptides for pharmaceutical applications. Its unique composition allows for the creation of specific peptide sequences that can target various biological pathways and mechanisms, potentially leading to the development of new drugs.
Used in Biochemical Research:
In biochemical research, Boc-Phe-Ser-Ome serves as a valuable tool for studying protein synthesis and the role of specific amino acids in biological processes. Its presence in experimental setups can help researchers understand the interactions between different biomolecules and their functions within the body.
Used in Peptide Synthesis:
Boc-Phe-Ser-Ome is used as a protected amino acid in peptide synthesis to facilitate the stepwise assembly of peptide chains. The Boc group temporarily masks the amino group, preventing unwanted side reactions and allowing for the controlled addition of amino acids to form the desired peptide sequence.
Used in Drug Design:
Boc-Phe-Ser-Ome is utilized in drug design to create novel bioactive peptides with specific therapeutic properties. Its incorporation into peptide structures can enhance the stability, bioavailability, and target specificity of peptide-based drugs, potentially leading to more effective treatments for various diseases.
Overall, Boc-Phe-Ser-Ome is a multifaceted compound with applications spanning across the pharmaceutical, biochemical research, and drug design industries, highlighting its importance in the development of innovative therapeutic agents and scientific understanding.

InChI:InChI=1/C18H26N2O6/c1-18(2,3)26-17(24)20-13(10-12-8-6-5-7-9-12)15(22)19-14(11-21)16(23)25-4/h5-9,13-14,21H,10-11H2,1-4H3,(H,19,22)(H,20,24)

Upstream product

• 2788-84-3 (S)-serine methyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 5680-80-8 methyl (2S)-2-amino-3-hydroxypropanoate hydrochloride 
• 3674-06-4 Boc-Phe-ONSu 
• 1280225-79-7 2,4-dioxo-3-azaspiro[5.5]undecan-3-yl (tert-butoxycarbonyl)-L-phenylalaninate 

Downstream Products

• 817624-22-9 Boc-Phe-Gly(OAc)-OMe 
• 32899-48-2 Boc-Phe-Ser-NHNH₂ 
• 142342-86-7 (R)-2-((S)-1-tert-Butoxycarbonylamino-2-phenyl-ethyl)-4,5-dihydro-oxazole-4-carboxylic acid methyl ester 
• 170454-77-0 (R)-2-((S)-2-tert-Butoxycarbonylamino-3-phenyl-propionylamino)-3-iodo-propionic acid methyl ester 
• 2531-47-7 H-Phe-Ser-Pro-Phe-Arg(NO₂)-OBzl 
• 135924-40-2 Boc-Phe-Gly(SEt)-OMe 
• 142342-86-7 methyl (4S,1'S)-2-[1-(tert-butoxycarbonylamino)-2-phenylethyl]-4,5-dihydrooxazole-4-carboxylate 
• 368424-85-5 Phenylalanylserine methyl ester 
• 135112-41-3 Boc-Phe-Ser-5-Ava-Arg(NO₂)-OBzl 
• 76546-53-7 Z-Arg(NO₂)-5-Ava-Gly-Phe-Ser-Pro-Phe-Arg(NO₂)-OBzl 
• 135112-42-4 Z-Arg(NO₂)-Pro-Pro-Gly-Phe-Ser-5-Ava-Arg(NO₂)-OBzl 
• 76523-60-9 H-Arg-5-Ava-Gly-Phe-Ser-Pro-Phe-Arg-OH 
• 135214-54-9 H-Arg-Pro-Pro-Gly-Phe-Ser-5-Ava-Arg-OH 
• 76523-58-5 H-5-Ava-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH 

Relevant articles and documents

Synthesis and Biological Evaluation of CF3Se-Substituted α-Amino Acid Derivatives

Several CF3Se-substituted α-amino acid derivatives, such as (R)-2-amino-3-((trifluoromethyl)selanyl)propanoates (5 a/6 a), (S)-2-amino-4-((trifluoromethyl)selanyl)butanoates (5 b/6 b), (2R,3R)-2-amino-3-((trifluoromethyl)selanyl)butanoates (5 c/6 c), (R)-2-((S)-2-amino-3-phenylpropanamido)-3-((trifluoromethyl)selanyl)propanoates (11 a/12 a), and (R)-2-(2-aminoacetamido)-3-((trifluoromethyl)selanyl)propanoates (11 b/12 b), were readily synthesized from natural amino acids and [Me4N][SeCF3]. The primary in vitro cytotoxicity assays revealed that compounds 6 a, 11 a and 12 a were more effective cell growth inhibitors than the other tested CF3Se-substituted derivatives towards MCF-7, HCT116, and SK-OV-3 cells, with their IC50 values being less than 10 μM for MCF-7 and HCT116 cells. This study indicated the potentials of CF3Se moiety as a pharmaceutically relevant group in the design and synthesis of novel biologically active molecules.

Promiscuous Enzymes Cooperate at the Substrate Level en Route to Lactazole A

Enzymes involved in the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs) often have relaxed specificity profiles and are able to modify diverse substrates. When several such enzymes act together during precursor peptide maturation, a multitude of products can form, yet usually the biosynthesis converges on a single natural product. For the most part, the mechanisms controlling the integrity of RiPP assembly remain elusive. Here, we investigate the biosynthesis of lactazole A, a model thiopeptide produced by five promiscuous enzymes from a ribosomal precursor peptide. Using our in vitro thiopeptide production (FIT-Laz) system, we determine the order of biosynthetic events at the individual modification level and supplement this study with substrate scope analysis for participating enzymes. Our results reveal an unusual but well-defined assembly process where cyclodehydration, dehydroalanine formation, and azoline dehydrogenation events are intertwined due to minimal substrate recognition requirements characteristic of every lactazole enzyme. Additionally, each enzyme plays a role in directing LazBF-mediated dehydroalanine formation, which emerges as the central theme of the assembly process. Cyclodehydratase LazDE discriminates a single serine residue for azoline formation, leaving the remaining five as potential dehydratase substrates. Pyridine synthase LazC exerts kinetic control over LazBF to prevent the formation of overdehydrated thiopeptides, whereas the coupling of dehydrogenation to dehydroalanine installation impedes generation of underdehydrated products. Altogether, our results indicate that substrate-level cooperation between the biosynthetic enzymes maintains the integrity of lactazole assembly. This work advances our understanding of RiPP biosynthesis processes and facilitates thiopeptide bioengineering.

Singlet Oxygen Photooxidation of Peptidic Oxazoles and Thiazoles

Oxazoles and thiazoles are commonly found moieties in nonribosomal peptides (NRPs) and ribosomally synthesized post-translationally modified peptides (RiPPs), which are important biomolecules present in the environment and in natural waters. From previous studies, they seem susceptible to oxidation by singlet oxygen (1O2); therefore, we designed and synthesized model oxazole- and thiazole-peptides and measured their1O2 bimolecular reaction rate constants, showing slow photooxidation under environmental conditions. We reasoned their stability through the electron-withdrawing effect of the carboxamide substituent. Reaction products were elucidated and support a reaction mechanism involving cycloaddition followed by a series of rearrangements. The first1O2 bimolecular reaction rate constant for a RiPP, the thiazole-containing peptide Aerucyclamide A, was measured and found in good agreement with the model peptide's rate constant, highlighting the potential of using model peptides to study the transformations of other environmentally relevant NRPs and RiPPs.

3-Azaspiro[5,5]undecan-2,4-dioxo-3-yl diphenyl phosphate (ASUD-diphenyl phosphate), a new reagent for the synthesis of the N-protected amino acid-ASUD ester

A new reagent, 3-azaspiro[5,5]undecan-2,4-dioxo-3-yl diphenyl phosphate (ASUD-diphenyl phosphate) is described for the synthesis of N-protected amino acid-ASUD esters which are active esters useful in the synthesis of peptides. This compound was synthesized by reacting N-hydroxy-3-azaspiro[5,5]undecane-2,4-dione (HO-ASUD) with diphenyl chlorophosphate in the presence of a base at room temperature and was obtained in high yields. The ASUD-diphenyl phosphate reagent reacts with N-protected amino acids under mild conditions to give the corresponding ASUD active esters, while preserving the enantiomeric purity of the amino acid. The new reagent is a stable crystalline compound and eliminates the need for DCC, a potent skin allergen, used previously for the synthesis of N-protected amino acid-ASUD ester.

Combinatorial synthesis of oxazol-thiazole bis-heterocyclic compounds

A combinatorial library of novel oxazol-thiazole bis-heterocycles was synthesized in good to excellent overall yields with high purity using a solution and solid-phase parallel synthesis approach. Oxazole amino acids, prepared from serine methyl ester and

Parallel synthesis of bis-oxazole peptidomimetics

The parallel synthesis of bis-oxazole peptidomimetics starting from Boc-aminoacids and Serine-methyl ester is described. This work presents the synthesis of oxazole aminoacid building blocks in solution phase and their utilization for the solid phase pept

CIDOFOVIR PEPTIDE CONJUGATES AS PRODRUGS

Cidofovir-based compounds having an amino acid, dipeptide or tripeptide attached to a cidofovir or cyclic cidofovir framework. The compounds show enhanced oral bioavailability and increased binding to the PepT1 transporter. The present invention also provides compositions and methods for treating virus infections, and a method of preparing cidofovir.

Pd(0)-catalyzed Heck-type arylation of didehydropeptides

Pd(0)-catalyzed Heck-type arylation of several didehydropeptides has been studied and the process has been found to be a viable method for the synthesis of the corresponding arylated products stereoselectively but in moderate yields. Copyright Taylor & Fr

Total synthesis of trunkamide A, a novel thiazoline-based prenylated cyclopeptide metabolite from Lissoclinum sp.

Full details of a total synthesis of the doubly prenylated cyclic peptide trunkamide A of marine origin, and also its C45 epimer, are described.

Allyltrichlorostannane additions to chiral dipeptide aldehydes

The first examples of successful allylsilane additions to chiral dipeptide aldehydes are described. Treatment of allylsilanes with tin tetrachloride at room temperature affords allyltrichlorostannane intermediates that reacts with dipeptide aldehydes to give 1,2-syn-homoallylic alcohols, potential intermediates for the synthesis of hydroxyethylene dipeptide isosteres.