103882-09-3

Basic information

• Product Name: BOC-P-IODO-DL-PHE-OH
• Synonyms: BOC-4-IODO-DL-PHENYLALANINE;BOC-DL-PHE(4-I)-OH;BOC-DL-PHE(P-I)-OH;BOC-P-IODO-DL-PHENYLALANINE;BOC-P-IODO-DL-PHE-OH;N-T-BUTOXYCARBONYL-P-IODO-DL-PHENYLALANINE;Boc-DL-4-Iodophenylalanine;N-Boc-4-Iodo-DL-phenylalanine
• CAS NO: 103882-09-3
• Molecular Formula: C₁₄H₁₈INO₄
• Molecular Weight: 391.2
• Mol File: 103882-09-3.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: BOC-P-IODO-DL-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: BOC-P-IODO-DL-PHE-OH(103882-09-3)
• EPA Substance Registry System: BOC-P-IODO-DL-PHE-OH(103882-09-3)

Safety Data

• Hazardous Substances Data: 103882-09-3(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
BOC-P-IODO-DL-PHE-OH is used as a building block for the synthesis of pharmaceutical compounds, leveraging its reactivity and the protective nature of the BOC group to facilitate the creation of complex peptide structures and other organic molecules with potential therapeutic applications.
Used in Chemical Research:
In the field of chemical research, BOC-P-IODO-DL-PHE-OH is utilized as a precursor in the development of new organic molecules. Its unique structure allows for the exploration of novel chemical reactions and the synthesis of compounds with specific properties for various applications.
Used in Organic Synthesis:
BOC-P-IODO-DL-PHE-OH is employed as a key intermediate in organic synthesis, particularly for the preparation of specialty chemicals, agrochemicals, and other complex organic molecules. Its iodo substituent and BOC protection make it a valuable component in the synthesis of target molecules with specific functional groups and reactivity profiles.

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 1991-81-7 4-iodo-L-phenylalanine 
• 16004-15-2 1-bromomethyl-4-iodobenzene 
• 102831-44-7 diethyl tert-butoxycarbonylaminomalonate 
• 7087-68-5 N-ethyl-N,N-diisopropylamine 
• 63-91-2 L-phenylalanine 

Downstream Products

• 796072-33-8 N-tert-butyloxycarbonyl-(L)4-iodophenylalanine methyl ester 
• 135414-03-8 N^α-tert-Butoxycarbonyl-p-cyano-D,L-phenylalanine 
• 796072-34-9 2-tert-butoxycarbonylamino-3-(4'-dibenzofuran-4-yl-biphenyl-4-yl)-propanoic acid methyl ester 
• 137452-47-2 N-Boc-4-formyl-L-phenylalanine 
• 79385-56-1 methyl {(S)-2-[(tert-butoxycarbonyl)amino]-3-(4-iodophenyl)propanoyl}-L-phenylalaninate 
• 1026064-05-0 3-hydroxy-O-methyl-N-<4-iodo-N-<(1,1-dimethylethoxy)carbonyl>-L-phenylalanyl>-L-tyrosine methyl ester 
• 113850-81-0 (S)-2-tert-Butoxycarbonylamino-3-{4-[4-((S)-2-tert-butoxycarbonylamino-2-methoxycarbonyl-ethyl)-phenylsulfanyl]-phenyl}-propionic acid 
• 108826-83-1 Boc-Phe(I)-Gaba-OTmse 
• 82565-70-6 Boc-Phe(4-I)-Gly-Leu-Met-NH₂ 
• 178896-43-0 5-[(S)-2-tert-Butoxycarbonylamino-3-(4-iodo-phenyl)-propionylamino]-isophthalic acid dibenzyl ester 
• 113850-76-3 N-(tert-butoxycarbonyl)-4-iodo-L-phenylalanine methyl ester 

Relevant articles and documents

Synthesis and Explosion Hazards of 4-Azido- l -phenylalanine

A reliable, scalable, cost-effective, and chromatography-free synthesis of 4-azido-l-phenylalanine beginning from l-phenylalanine is described. Investigations into the safety of the synthesis reveal that the Ullman-like Cu(I)-catalyzed azidation step does not represent a significant risk. The isolated 4-azido-l-phenylalanine product, however, exhibits previously undocumented explosive characteristics.

Development of potent and selective Cathepsin C inhibitors free of aortic binding liability by application of a conformational restriction strategy

Cathepsin C plays a key role in the activation of several degradative enzymes linked to tissue destruction in chronic inflammatory and autoimmune diseases. Therefore, Cathepsin C inhibitors could potentially be effective therapeutics for the treatment of diseases such as chronic obstructive pulmonary disease (COPD) or acute respiratory distress syndrome (ARDS). In our efforts towards the development of a novel series of Cathepsin C inhibitors, we started working around AZD5248 (1), an α-amino acid based scaffold having potential liability of aortic binding. A novel series of amidoacetonitrile based Cathepsin C inhibitors were developed by the application of a conformational restriction strategy on 1. In particular, this work led to the development of a potent and selective Cathepsin C inhibitor 3p, free of aortic binding liability.

Nickel-Catalyzed Asymmetric Synthesis of α-Arylbenzamides

A nickel-catalyzed asymmetric reductive hydroarylation of vinyl amides to produce enantioenriched α-arylbenzamides is reported. The use of a chiral bisimidazoline (BIm) ligand, in combination with diethoxymethylsilane and aryl halides, enables the regioselective introduction of aryl groups to the internal position of the olefin, forging a new stereogenic center α to the N atom. The use of neutral reagents and mild reaction conditions provides simple access to pharmacologically relevant motifs present in anticancer, SARS-CoV PLpro inhibitors, and KCNQ channel openers.

Photoinduced Hydroxylation of Organic Halides under Mild Conditions

Presented in this paper is photoinduced hydroxylation of organic halides, providing a mild access to a range of functionalized phenols and aliphatic alcohols. These reactions generally proceed under mild reaction conditions with no need for a photocatalyst or a strong base and show a wide substrate scope as well as excellent functional group tolerance. This work highlights the unique role of NaI that allows a challenging transformation to proceed under mild reaction conditions.

Structure-Activity Relationships of cyclo(l -Tyrosyl- l -tyrosine) Derivatives Binding to Mycobacterium tuberculosis CYP121: Iodinated Analogues Promote Shift to High-Spin Adduct

A series of analogues of cyclo(l-tyrosyl-l-tyrosine), the substrate of the Mycobacterium tuberculosis enzyme CYP121, have been synthesized and analyzed by UV-vis and electron paramagnetic resonance spectroscopy and by X-ray crystallography. The introduction of iodine substituents onto cyclo(l-tyrosyl-l-tyrosine) results in sub-μM binding affinity for the CYP121 enzyme and a complete shift to the high-spin state of the heme FeIII. The introduction of halogens that are able to interact with heme groups is thus a feasible approach to the development of next-generation, tight binding inhibitors of the CYP121 enzyme, in the search for novel antitubercular compounds.

METHOD FOR PREPARING L-BPA

Provided is a method for preparing L-BPA, which includes steps of: reacting N-protected (S)-4-halophenylalanine of Formula I, a boronating agent, Grignard reagent and bis(2-methylaminoethyl)ether to obtain a reaction mixture, wherein the reaction mixture comprises N-protected (S)-4-boronophenylalanine of Formula II and the R2 group represents a protecting group; isolating the N-protected (S)-4-boronophenylalanine from the reaction mixture; and deprotecting the R2 group of the N-protected (S)-4-boronophenylalanine to obtain L-BPA, wherein the L-BPA has a structure of Formula III.

A simple, efficient, regioselective and one-pot preparation of N-hydroxy- and N-O-protected hydroxyindoles via cycloaddition of nitrosoarenes with alkynes. Synthetic scope, applications and novel by-products

The thermal reaction between nitrosoarenes and alkynes under alkylating conditions produces N-alkoxyindoles as the major products in moderate to good yields and excellent regioselectivity. Various electrophiles are used affording different N-O-protected hydroxyindoles in a multi-component fashion. Privileged acetylenic substrates used in reactions with substituted nitrosoarenes are arylalkynes or propiolates. Potentially bioactive compounds and other classes of highly functionalizable indole products were prepared. Reactions between o-carbomethoxy-nitrosoarenes and arylacetylenes provided tricyclic compounds containing an acylaziridine indoline skeleton.

Self-liganded Suzuki-Miyaura coupling for site-selective protein PEGylation

Building with PEGs: PEG-boronic acids, in the presence of simple Pd sources, are capable of acting as direct and effective Suzuki reagents in 70-98 % yield. When combined with non-natural amino acids, they allow efficient and direct, site-selective PEGylation of proteins at predetermined positions under biologically compatible conditions without the need for exogenous ligands.

C-Glycosyl amino acids through hydroboration-cross-coupling of exo-glycals and their application in automated solid-phase synthesis

O-Glycosylation is one of the most important post-translational modifications of proteins. The attachment of carbohydrates to the peptide backbone influences the conformation as well as the solubility of the conjugates and can even be essential for binding to specific ligands in cell-cell interactions or for active transport over membranes. This makes glycopeptides an interesting class of compounds for medical applications. To enhance the long-term availability of these molecules in vivo, the stabilization of the glycosidic bond between the amino acid residue and the carbohydrate is of interest. The described modular approach affords β-linked C-glycosyl amino acids by a sequence of Petasis olefination of glyconolactones, stereoselective hydroboration and a mild B-alkyl-Suzuki coupling reaction. The coupling products were transformed to C-glycosyl amino acid building-blocks suitable for solid-phase synthesis and successfully incorporated into a partial sequence of the tumor-associated MUC1-glycopeptide. The resulting C-glycopeptides are candidates for the development of long-term stable mimics of O-glycopeptide vaccines. Copyright

Palladium-mediated cell-surface labeling

Benign C-C bond formation at various sites in cell-surface channels has been achieved through Suzuki-Miyaura coupling of genetically positioned unnatural amino acids containing aryl halide side chains. This enabled site-selective cell surface manipulation of Escherichia coli; the phosphine-free catalyst caused no cell death at required Pd loadings, suggesting future in vivo application of catalytic metal-mediated bond formation in more complex organisms.