20829-55-4

Usage

Uses

Used in Pharmaceutical Applications:
CYCLO(-TRP-TRP) is used as a cytotoxic agent for its moderate cytotoxic activities against HeLa PC3 lines. This property makes it a promising candidate for the development of new drugs targeting cancer cells.
Used in Biotechnological Applications:
CYCLO(-TRP-TRP) is used as a biotechnological tool for its potential applications in the development of genetically engineered strains and the production of essential amino acids, such as L-Tryptophan.
Used in Chemical Research:
As a light yellow powder with unique chemical properties, CYCLO(-TRP-TRP) can be utilized in chemical research to study its structure, properties, and potential interactions with other molecules, which may lead to the discovery of new applications and uses in various industries.

Upstream product

• 73-22-3 L-Tryptophan 
• 4299-69-8 L-tryptophane benzyl ester 
• 4299-70-1 L-tryptophan methyl ester 
• 7524-52-9 (S)-tryptophan methyl ester hydrochloride 
• 7432-21-5 N-carbobenzyloxy-L-tryptophane 
• 17689-58-6 N-(benzyloxycarbonyl)-L-tryptophanyl-L-tryptophan methyl ester 
• 81387-96-4 (S,S)-methyl 2-[2-amino-3-(indol-3-yl)propionylamino]-3-(indol-3-yl)propanoate 
• 13139-14-5 Boc-Trp-OH 
• 72254-56-9 (S,S)-methyl 2-[2-tert-butoxycarbonylamino-3-(indol-3-yl)-propionylamino]-3-(indol-3-yl)propanoate 

Downstream Products

• 73-22-3 L-Tryptophan 

Relevant academic research and scientific papers

The structure and conformation of the tryptophanyl diketopiperazines cyclo(Trp-Trp)·C2H6SO and cyclo(Trp-Pro)

The structure and conformation of the cyclic dipeptides [cyclo(L-Trp-L-Trp)·C2H6SO] and cyclo(L-Trp-L-Pro) have been investigated with X-ray crystallographic and spectroscopic methods. Cyclo(L-tryptophanyl-L-tryptophanyl)·DMSO solvate crystallized in the space group P212121 with cell dimensions a = 6.193(2), b = 11.545(3), c = 31.117(4) A. The crystal structure is stabilized by four hydrogen bonds (three intermolecular hydrogen bonds and one intramolecular bond). The first intermolecular bond is between the oxygen of DMSO and the nitrogen of indole ring 2, in contrast to the second intramolecular hydrogen bond between the nitrogen of indole ring 1 and the oxygen of DMSO. The two remaining intermolecular hydrogen bonds are between the nitrogens of the DKP ring and the carbonyl oxygens of the DKP ring. The values of X1A1 (-45.764) and X1A2 (67.437) indicate an extended side chain conformation for Trp residue 1 (EN) and a folded conformation for Trp residue 2. The DKP ring is more planar than in other cyclic dipeptide compounds (φ1 = 11.414, ψ1 = -7.516, φ2 = 12.471, and ψ2 = -8.256). In cyclo(L-Trp-L-Trp) the Cβ resonance of L-tryptophan (29.88 ppm) is shifted upfield 0.82 ppm when compared with the same resonance in cyclo(L-Trp-L-Gly) (30.7 ppm) and cyclo(L-Leu-L-Trp) (30.7 ppm). Two conformations of cyclo(Trp-Pro) crystallized in the space group P1 with cell dimensions a = 5.422(1), b = 9.902(1), c = 13.443(2) A, α = 80.42(1), β = 78.61(1), and γ = 89.13(1)°. The conformation of the backbone and the orientation of the aromatic side chains for these conformers are very similar. The DKP rings for both conformers adopt a typical boat conformation in contrast to the flattened chair conformation observed for cyclo(Tyr-Pro) and cyclo(Phe-F-Pro). The tryptophan side chains of these conformers are folded towards the diketopiperazine (DKP) ring. The pyrrolidine ring for conformer 1 can be described as an envelope (Cs-Cβ-endo) conformation in contrast to the pyrrolidine ring symmetry for conformer 2 which is an intermediate between Cs and C2 rather than pure Cs for the proline ring with Cβ-endo and Cγ-exo with respect to C′. The two prolyl rings are puckered at the β-carbon atoms which deviate from the best planes defined by the four remaining atoms. The crystal structures are stabilized by four intermolecular hydrogens bonds. An intermolecular bond between the nitrogen of the indole ring (conformer 1) and the carbonyl oxygen of the DKP ring (conformer 2) was observed. The second hydrogen bond is between the nitrogen of the indole ring (conformer 2) and the carbonyl oxygen of the DKP ring (conformer 1). The last two hydrogens involve the carbonyl oxygens of the DKP rings and the nitrogens of the DKP rings [carbonyl oxygen of DKP ring (conformer 1) - nitrogen of DKP ring (conformer 2); nitrogen of DKP ring (conformer 1) - carbonyl oxygen of DKP ring (conformer 2)].

Total Synthesis of Homo-and Heterodimeric Bispyrrolidinoindoline Dioxopiperazine Natural Products

Total synthesis and structural confirmation of homo-and heterodimeric bispyrrolidinoindoline dioxopiperazine alkaloids isolated from fungi and bacteria, namely, ditryptoleucine A, ditryptoleucine B (11), the N,N′-bis-demethylated analogue (+)-12, (-)-dibrevianamide F (13), (-)-SF-5280-451 (14), tetratryptomycin A (15), (-)-Tryprophenaline (17), and (-)-SF-5280-415 (18), has been carried out starting from the corresponding bispyrrolidinoindolines derived from tryptophan. Our efforts to synthesize all possible diastereomers of the natural ditryptoleucine isolates uncovered structural factors that determine the rate and efficiency of dioxopiperazine ring formation, leading in some cases to mixtures of diastereomers by concomitant epimerization, to the formation of their putative monomeric dioxopiperazine dipeptide biogenetic precursors, and to the alternative formation of a dimer with a fused 1,3,5-Triazepan-6-one heterocycle.

Synergism between genome sequencing, tandem mass spectrometry and bio-inspired synthesis reveals insights into nocardioazine B biogenesis

Marine actinomycete-derived natural products continue to inspire chemical and biological investigations. Nocardioazines A and B (3 and 4), from Nocardiopsis sp. CMB-M0232, are structurally unique alkaloids featuring a 2,5-diketopiperazine (DKP) core functionalized with indole C3-prenyl as well as indole C3- and N-methyl groups. The logic of their assembly remains cryptic. Bioinformatics analyses of the Nocardiopsis sp. CMB-M0232 draft genome afforded the noz cluster, split across two regions of the genome, and encoding putative open reading frames with roles in nocardioazine biosynthesis, including cyclodipeptide synthase (CDPS), prenyltransferase, methyltransferase, and cytochrome P450 homologs. Heterologous expression of a twelve gene contig from the noz cluster in Streptomyces coelicolor resulted in accumulation of cyclo-l-Trp-l-Trp DKP (5). This experimentally connected the noz cluster to indole alkaloid natural product biosynthesis. Results from bioinformatics analyses of the noz pathway along with challenges in actinomycete genetics prompted us to use asymmetric synthesis and mass spectrometry to determine biosynthetic intermediates in the noz pathway. The structures of hypothesized biosynthetic intermediates 5 and 12-17 were firmly established through chemical synthesis. LC-MS and MS-MS comparison of these synthetic compounds with metabolites present in chemical extracts from Nocardiopsis sp. CMB-M0232 revealed which of these hypothesized intermediates were relevant in the nocardioazine biosynthetic pathway. This established the early and mid-stages of the biosynthetic pathway, demonstrating that Nocardiopsis performs indole C3-methylation prior to indole C3-normal prenylation and indole N1′-methylation in nocardioazine B assembly. These results highlight the utility of merging bioinformatics analyses, asymmetric synthetic approaches, and mass spectrometric metabolite profiling in probing natural product biosynthesis.

Three types of induced tryptophan optical activity compared in model dipeptides: Theory and experiment

The tryptophan (Trp) aromatic residue in chiral matrices often exhibits a large optical activity and thus provides valuable structural information. However, it can also obscure spectral contributions from other peptide parts. To better understand the indu

Investigation of reaction mechanism of amino acids and phosphorus trichloride by 31P NMR and ESI-MS/MS

The reaction of amino acids and phosphorus trichloride in THF was studied by 31P NMR tracing and ESI-MS/MS. A series of hydridophoranes and cyclic dipeptides were obtained. The reaction presented interesting diversity and the reaction mechanism was proposed. The mechanism suggests that phosphorus plays an important role in the synthesis of amino acid hydridophorane and cyclic dipeptides. The results also show that 31P NMR and ESI-MS/MS are useful tools for the investigation of reaction mechanism. Copyright

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.

Synthesis and separation of L-trytophan oligo-peptides assisted by phosphorus oxychloride

With the assistance of inorganic phosphorus, α-amino acids could self-assemble into a series of oligopeptides, so it could provide a new route to synthesize peptides. In this paper, the self-assembly reaction of L-trytophan mediated by phosphorus oxychloride was monitored by using ESI-MS. The proper condition of the self-assembly reaction of L-Try was reported. The reaction products were purified by RP-HPLC and the fragmentation pathway for L-Try oligo-peptides were analyzed by using ESI-MS/MS.

Engineered transaminopeptidase, aminolysin-S for catalysis of peptide bond formation to give linear and cyclic dipeptides by one-pot reaction

Aminopeptidase from Streptomyces thermocyaneoviolaceus NBRC14271 was engineered into transaminopeptidase and used to catalyze an aminolysis reaction to give linear and cyclic dipeptides from cost-effective substrates such as the ester derivatives of amino

Fragmentation of deprotonated cyclic dipeptides by electrospray ionization mass spectrometry

The fragmentation pathways of deprotonated cyclic dipeptides have been studied by electrospray ionization multi-stage mass spectrometry (ESI-MSn) in negative mode. The results showed that the fragmentation pathways of deprotonated cyclic dipeptides depend

Participation of aromatic side chains in diketopiperazine ensembles

This study probes the beneficial role of aromatic side chains in peptide self-assembly by choosing four diketopiperazine model systems variably composed of glycine, proline, phenylalanine, and tryptophan residues.