80206-30-0

Usage

Uses

Used in Dietary Supplements:
L-TRYPTOPHAN is used as a dietary supplement for individuals seeking potential benefits such as improved sleep, mood enhancement, and reduced symptoms of depression and anxiety. It is particularly beneficial for those who may not consume enough protein-rich foods in their diet.
Used in Pharmaceutical Applications:
L-TRYPTOPHAN is used in the pharmaceutical industry for its role in the synthesis of niacin, a B-vitamin important for energy production and metabolism. It may also be utilized in the development of medications targeting sleep disorders, mood regulation, and mental health conditions.
Used in Nutraceutical Industry:
In the nutraceutical industry, L-TRYPTOPHAN is used as an ingredient in various health products and supplements that aim to promote overall well-being and support cognitive and emotional health.

InChI:InChI=1/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1

Upstream product

• 149828-46-6 N^α-ethoxycarbonyl-DL-tryptophan-ethyl ester 
• 1218-34-4 N-acetyl-DL-tryptophan 
• 2901-79-3 2-(benzoylamino)-3-(indol-3-yl)propanoic acid 
• 120-72-9 indole 
• 302-84-1 serin 
• 3981-36-0 3-chloro-DL-alanine 
• 81084-87-9 isopropyl (+/-)-tryptophanoate 
• 63767-98-6 N^α-dithiocarboxy-DL-tryptophan 
• 7647-01-0 hydrogenchloride 
• 7732-18-5 water 
• 17507-43-6 2-benzoylamino-3-indol-3-yl-acrylic acid 
• 7303-49-3 DL-tryptophan methyl ester 
• 392-12-1 Indole-3-pyruvic acid 
• 127-17-3 2-oxo-propionic acid 

Downstream Products

• 16765-80-3 1-benzyl-β-carboline 
• 7303-49-3 DL-tryptophan methyl ester 
• 93873-46-2 N^α-(4-methanesulfonyl-2-nitro-phenyl)-DL-tryptophan 
• 3262-57-5 N^α-(N-benzyloxycarbonyl-glycyl)-DL-tryptophan 
• 79189-76-7 N²-(chloroacetyl)-DL-tryptophan 
• 67805-23-6 9H-1(4'-Dimethylaminophenyl)-3-carboxy-1,2,3,4-tetrahydropyrido<3,4-b>indol 
• 149586-34-5 N^α-benzenesulfonyl-tryptophan 
• 85979-07-3 N^α-(N-acetyl-sulfanilyl)-DL-tryptophan 
• 23850-16-0 1-cyclohex-3-enyl-2,3,4,9-tetrahydro-1H-β-carboline-3-carboxylic acid 
• 121394-74-9 N^α-[1-(N-benzyloxycarbonyl-glycyl)-L-prolyl]-DL-tryptophan 
• 64403-52-7 N-(2-phenyl-naphtho[1,2-d]oxazole-5-sulfonyl)-tryptophan 
• 142907-00-4 Nⁱ-(4-phenylbutyl)-L-tryptophan 
• 86323-62-8 3-(1H-Indol-3-yl)-2-(4-nitro-benzoylamino)-propionic acid isopropyl ester 
• 86323-50-4 3-(1H-Indol-3-yl)-2-(4-nitro-benzoylamino)-propionic acid isopropyl ester 

Relevant academic research and scientific papers

Fabrication of mesoporous carbon tube and foam: Application as supports in enantio-selective separation of optically pure amino acid from racemates

The mesoporous monolithic carbon (MMC) foams and carbon tubes were newly fabricated in cmscale using the mixture of triblock copolymers and phenol/HCHO resin precursors. The regular mesoporosity were formed in the body of MMC foam and carbon fibers. In this work, the organic phases containing chiral ARCA adsorbent and a phase transfer catalyst were coated on the surfaces of mesoporous carbon support, and this ARCA/carbon mixture was adopted for the enantioselective separation of amino acid in the circulation system. (S)-ARCA coated MMC support showed high selcetivity up to 90% for the separation of D-type phenylalanine, serine and tryptophan from racemic mixtures.

Recreating the natural evolutionary trend in key microdomains provides an effective strategy for engineering of a thermomicrobial N-demethylase

N-demethylases have been reported to remove the methyl groups on primary or secondary amines, which could further affect the properties and functions of biomacromolecules or chemical compounds; however, the substrate scope and the robustness of N-demethylases have not been systematically investigated. Here we report the recreation of natural evolution in key microdomains of the Thermomicrobium roseum sarcosine oxidase (TrSOX), an N-demethylase with marked stability (melting temperature over 100 C) and enantioselectivity, for enhanced substrate scope and catalytic efficiency on -C-N-bonds. We obtained the structure of TrSOX by crystallization and X-ray diffraction (XRD) for the initial framework. The natural evolution in the nonconserved residues of key microdomains—including the catalytic loop, coenzyme pocket, substrate pocket, and entrance site—was then identified using ancestral sequence reconstruction (ASR), and the substitutions that accrued during natural evolution were recreated by site-directed mutagenesis. The single and double substitution variants catalyzed the N-demethylation of N-methyl-L-amino acids up to 1800- and 6000-fold faster than the wild type, respectively. Additionally, these single substitution variants catalyzed the terminal N-demethylation of non-amino-acid compounds and the oxidation of the main chain -C-N- bond to a -C=N- bond in the nitrogen-containing heterocycle. Notably, these variants retained the enantioselectivity and stability of the initial framework. We conclude that the variants of TrSOX are of great potential use in N-methyl enantiomer resolution, main-chain Schiff base synthesis, and alkaloid modification or degradation.

Highly Stable Zr(IV)-Based Metal-Organic Frameworks for Chiral Separation in Reversed-Phase Liquid Chromatography

Separation of racemic mixtures is of great importance and interest in chemistry and pharmacology. Porous materials including metal-organic frameworks (MOFs) have been widely explored as chiral stationary phases (CSPs) in chiral resolution. However, it remains a challenge to develop new CSPs for reversed-phase high-performance liquid chromatography (RP-HPLC), which is the most popular chromatographic mode and accounts for over 90% of all separations. Here we demonstrated for the first time that highly stable Zr-based MOFs can be efficient CSPs for RP-HPLC. By elaborately designing and synthesizing three tetracarboxylate ligands of enantiopure 1,1′-biphenyl-20-crown-6, we prepared three chiral porous Zr(IV)-MOFs with the framework formula [Zr6O4(OH)8(H2O)4(L)2]. They share the same flu topological structure but channels of different sizes and display excellent tolerance to water, acid, and base. Chiral crown ether moieties are periodically aligned within the framework channels, allowing for stereoselective recognition of guest molecules via supramolecular interactions. Under acidic aqueous eluent conditions, the Zr-MOF-packed HPLC columns provide high resolution, selectivity, and durability for the separation of a variety of model racemates, including unprotected and protected amino acids and N-containing drugs, which are comparable to or even superior to several commercial chiral columns for HPLC separation. DFT calculations suggest that the Zr-MOF provides a confined microenvironment for chiral crown ethers that dictates the separation selectivity.

COMPOUNDS AND METHODS FOR SELECTIVE C-TERMINAL LABELING

The present disclosure relates to compounds and methods for selective C-terminal functionalization of peptides. In certain embodiments, the compounds have improved water-solubility, and are suitable for use in connection with peptide sequencing methodologies.

Biocatalysts from cyanobacterial hapalindole pathway afford antivirulent isonitriles against MRSA

Abstract: The emergence of resistance to frontline antibiotics has called for novel strategies to combat serious pathogenic infections. Methicillin-resistant Staphylococcus aureus [MRSA] is one such pathogen. As opposed to traditional antibiotics, bacteriostatic anti-virulent agents disarm MRSA, without exerting pressure, that cause resistance. Herein, we employed a thermophilic Thermotoga maritima tryptophan synthase (TmTrpB1) enzyme followed by an isonitrile synthase and Fe(II)-α-ketoglutarate-dependent oxygenase, in sequence as biocatalysts to produce antivirulent indole vinyl isonitriles. We report on conversion of simple derivatives of indoles to their C3-vinyl isonitriles, as the enzymes employed here demonstrated broader substrate tolerance. In toto, eight distinct L-Tryptophan derived α-amino acids (7) were converted to their bioactive vinyl isonitriles (3) by action of an isonitrile synthase (WelI1) and an Fe(II)-α-ketoglutarate-dependent oxygenase (WelI3) yielding structural variants possessing antivirulence against MRSA. These indole vinyl isonitriles at 10 μg/mL are effective as antivirulent compounds against MRSA, as evidenced through analysis of rabbit blood hemolysis assay. Based on a homology modelling exercise, of enzyme-substrate complexes, we deduced potential three dimensional alignments of active sites and glean mechanistic insights into the substrate tolerance of the Fe(II)-α-ketoglutarate-dependent oxygenase. Graphic abstract: [Figure not available: see fulltext.]

Method for photolysis of amido bonds

The invention discloses a method for photo-splitting amido bonds, wherein the method is mild in reaction condition and can realize splitting of amido bonds by using illumination. The method for photo-splitting the amido bonds comprises the following steps: reacting 2,4-dinitrofluorobenzene with an amino group of a substance which contains alpha amino acid at the tail end and is shown as a structural formula I to generate a compound 1 represented by a structural formula II; and under light irradiation, carrying out amido bond cleavage reaction on the compound 1, wherein R1 is a side chain group of alpha-amino acid, and R2 is aryl, aliphatic hydrocarbon, -CH(R)-COOH or polypeptide.

Three diketomorpholines from a Penicillium sp. (strain G1071)

Three previously undescribed diketomorpholine natural products, along with the known phenalenones, herqueinone and norherqueinone, were isolated from the mycoparasitic fungal strain G1071, which was identified as a Penicillium sp. in the section Sclerotiora. The structures were established by analyzing NMR data and mass spectrometry fragmentation patterns. The absolute configurations of deacetyl-javanicunine A, javanicunine C, and javanicunine D, were assigned by examining ECD spectra and Marfey's analysis. The structural diversity generated by this fungal strain was interesting, as only a few diketomorpholines (~17) have been reported from nature.

Motobamide, an Antitrypanosomal Cyclic Peptide from a Leptolyngbya sp. Marine Cyanobacterium

Motobamide (1), a new cyclic peptide containing a C-prenylated cyclotryptophan residue, was isolated from a marine Leptolyngbya sp. cyanobacterium. Its planar structure was established by spectroscopic and MS/MS analyses. The absolute configuration was elucidated based on a combination of chemical degradations, chiral-phase HPLC analyses, spectroscopic analyses, and computational chemistry. Motobamide (1) moderately inhibited the growth of bloodstream forms of Trypanosoma brucei rhodesiense (IC50 2.3 μM). However, it exhibited a weaker cytotoxicity against normal human cells (IC50 55 μM).

METHODS FOR PRODUCING D-TRYPTOPHAN AND SUBSTITUTED D-TRYPTOPHANS

Single-module nonribosomal peptide synthetases (NRPSs) and NRPS-like enzymes activate and transform carboxylic acids in both primary and secondary metabolism; and are of great interest due to their biocatalytic potentials. The single-module NRPS IvoA is essential for fungal pigment biosynthesis. As disclosed herein, we show that IvoA catalyzes ATP-dependent unidirectional stereoinversion of L-tryptophan to D-tryptophan with complete conversion. While the stereoinversion is catalyzed by the epimerization (E) domain, the terminal condensation (C) domain stereoselectively hydrolyzes D-tryptophanyl-S-phosphopantetheine thioester and thus represents a noncanonical C domain function. Using IvoA, we demonstrate a biocatalytic stereoinversion/deracemization route to access a variety of substituted D-tryptophan analogs in high enantiomeric excess.

Targeted Isolation of Asperheptatides from a Coral-Derived Fungus Using LC-MS/MS-Based Molecular Networking and Antitubercular Activities of Modified Cinnamate Derivatives

Under the guidance of MS/MS-based molecular networking, four new cycloheptapeptides, namely, asperheptatides A-D (1-4), were isolated together with three known analogues, asperversiamide A-C (5-7), from the coral-derived fungus Aspergillus versicolor. The planar structures of the two major compounds, asperheptatides A and B (1 and 2), were determined by comprehensive spectroscopic data analysis. The absolute configurations of the amino acid residues were determined by advanced Marfey's method. The two structurally related trace metabolites, asperheptatides C and D (3 and 4), were characterized by ESI-MS/MS fragmentation methods. A series of new derivatives (8-26) of asperversiamide A (5) were semisynthesized. The antitubercular activities of 1, 2, and 5-26 against Mycobacterium tuberculosis H37Ra were also evaluated. Compounds 9, 13, 23, and 24 showed moderate activities with MIC values of 12.5 μM, representing a potential new class of antitubercular agents.