35737-15-6 | - Page 4 of 10 - Indole Building Blocks

Ostergaard, Soeren team published research on Angewandte Chemie, International Edition in 2021 | 35737-15-6

HPLC of Formula: 35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Previous studies have identified that indole-oxidases are present in P. putida, whose major ligands are heterocyclic substrates and have an interesting affinity when the substrate is indole. 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. These enzymes oxidize the ring so the substrate turns into Indigo. HPLC of Formula: 35737-15-6.

Ostergaard, Soeren;Paulsson, Johan F.;Kjaergaard Gerstenberg, Marina;Wulff, Birgitte S. research published 《 The design of a GLP-1/PYY dual acting agonist》, the research content is summarized as follows. The two gut hormones GLP-1 and PYY_3-36, which are both secreted from the L-cells upon food stimuli, have a stronger inhibitory effect on food intake when they are combined, compared to their individual effects as single agonists. Although they are not homologous and share no sequence similarity, we show that a GLP-1 analog can be designed to exhibit potent activity on both the Y₂ and GLP-1 receptors. Dual acting hybrid analogs were realized by designing truncated and potent Y₂ receptor PYY analogs, followed by integrating the critical residues into GLP-1. In this study, we show that one of these dual acting agonists acutely reduces food intake significantly more than the resp. mono-agonist counterparts.

Referemce:
Indole alkaloid derivatives as building blocks of natural products from Bacillus thuringiensis and Bacillus velezensis and their antibacterial and antifungal activity study,
Preparation of Indole Containing Building Blocks for the Regiospecific Construction of Indole Appended Pyrazoles and Pyrroles

Ozkose, Umut Ugur team published research on Journal of Applied Polymer Science in 2021 | 35737-15-6

Name: Fmoc-Trp-OH, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Ozkose, Umut Ugur;Gulyuz, Sevgi;Parlak Khalily, Melek;Ozcubukcu, Salih;Bozkir, Asuman;Tasdelen, Mehmet Atilla;Alpturk, Onur;Yilmaz, Ozgur research published 《 The synthesis of peptide-conjugated poly(2-ethyl-2-oxazoline)-b-poly(L-lactide) (PEtOx-b-PLA) polymeric systems through the combination of controlled polymerization techniques and click reactions》, the research content is summarized as follows. To optimize the therapeutic effect of pharmaceutical agents, drug delivery systems tailored from FDA-approved polymers like poly(L-lactide) (PLA) is an effective strategy. Because of their hydrophobic character, these systems greatly suffer from reduced circulation time thus, amphiphilic block copolymers became favorable to overcome this limitation. Of them, poly(oxazoline)-b-poly(L-lactide) are of choice as poly(oxazoline) (PEtOx) is compatible, biodegradable, while exhibiting min. cytotoxicity. To tailor selective drug targeting drug delivery systems, whereby their selectivity for tumor tissues is maximized, these polymers should be decorated with so-called tumor-homing agents, such as antibodies, peptides and so forth. To this respect, we designed a new block copolymer, allyl-poly(2-ethyl-2-oxazoline)-b-poly(L-lactide) allyl-(PEtOx-b-PLA) and its subsequent conjugation to tumor-homing peptides, peptide-18, and peptide-563 at the terminal position. In this manuscript, we report our synthetic route to obtain this building block and its conjugation to tumor-homing agents.

Pacifico, Salvatore team published research on Journal of Medicinal Chemistry in 2021 | 35737-15-6

Formula: C26H22N2O4, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

In addition to indoleacetic acid, indigo, and tryptophan, numerous compounds obtainable from plant or animal sources contain the indole molecular structure. 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. The best-known group of these compounds is the indole alkaloids, members of which have been isolated from plants representing more than 30 families. Formula: C26H22N2O4.

Pacifico, Salvatore;Albanese, Valentina;Illuminati, Davide;Marzola, Erika;Fabbri, Martina;Ferrari, Federica;Holanda, Victor A. D.;Sturaro, Chiara;Malfacini, Davide;Ruzza, Chiara;Trapella, Claudio;Preti, Delia;Lo Cascio, Ettore;Arcovito, Alessandro;Della Longa, Stefano;Marangoni, Martina;Fattori, Davide;Nassini, Romina;Calo, Girolamo;Guerrini, Remo research published 《 Novel mixed NOP/opioid receptor peptide agonists》, the research content is summarized as follows. The nociceptin/orphanin FQ (N/OFQ)/N/OFQ receptor (NOP) system controls different biol. functions including pain and cough reflex. Mixed NOP/opioid receptor agonists elicit similar effects to strong opioids but with reduced side effects. In this work, 31 peptides with the general sequence [Tyr/Dmt¹,Xaa⁵]N/OFQ(1-13)-NH₂ were synthesized and pharmacol. characterized for their action at human recombinant NOP/opioid receptors. The best results in terms of NOP vs. mu opioid receptor potency were obtained by substituting both Tyr¹ and Thr⁵ at the N-terminal portion of N/OFQ(1-13)-NH₂ with the noncanonical amino acid Dmt. [Dmt^1,5]N/OFQ(1-13)-NH₂ has been identified as the most potent dual NOP/mu receptor peptide agonist so far described. Exptl. data have been complemented by in silico studies to shed light on the mol. mechanisms by which the peptide binds the active form of the mu receptor. Finally, the compound exerted antitussive effects in an in vivo model of cough.

Paquette, Andre R. team published research on RSC Medicinal Chemistry in 2022 | 35737-15-6

Related Products of 35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Paquette, Andre R.;Payne, Sterling R.;McKay, Geoffrey A.;Brazeau-Henrie, Jordan T.;Darnowski, Micheal G.;Kammili, Anitha;Bernal, Federico;Mah, Thien-Fah;Gruenheid, Samantha;Nguyen, Dao;Boddy, Christopher N. research published 《 RpoN-Based stapled peptides with improved DNA binding suppress Pseudomonas aeruginosa virulence》, the research content is summarized as follows. Stapled peptides have the ability to mimic α-helixes involved in protein binding and have proved to be effective pharmacol. agents for disrupting protein-protein interactions. DNA-binding proteins such as transcription factors bind their cognate DNA sequences via an α-helix interacting with the major groove of DNA. We previously developed a stapled peptide based on the bacterial alternative sigma factor RpoN capable of binding the RpoN DNA promoter sequence and inhibiting RpoN-mediated expression in Escherichia coli. We have elucidated a structure-activity relationship for DNA binding by this stapled peptide, improving DNA binding affinity constants in the high nM range. Lead peptides were shown to have low toxicity as determined by their low hemolytic activity at 100 μM and were shown to have anti-virulence activity in a Galleria mellonella model of Pseudomonas aeruginosa infection. These findings support further preclin. development of stapled peptides as antivirulence agents targeting P. aeruginosa.

Patil, Nitin A. team published research on Frontiers in Chemistry (Lausanne, Switzerland) in 2022 | 35737-15-6

35737-15-6, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., SDS of cas: 35737-15-6

Indole, first isolated in 1866, has the molecular formula C8H7N, and it is commonly synthesized from phenylhydrazine and pyruvic acid, 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. although several other procedures have been discovered.Indole is a colourless solid having a pleasant fragrance in highly dilute solutions. It melts at 52.5° C (126.5° F). SDS of cas: 35737-15-6.

Patil, Nitin A.;Thombare, Varsha J.;Li, Rong;He, Xiaoji;Lu, Jing;Yu, Heidi H.;Wickremasinghe, Hasini;Pamulapati, Kavya;Azad, Mohammad A. K.;Velkov, Tony;Roberts, Kade D.;Li, Jian research published 《 An efficient approach for the design and synthesis of antimicrobial peptide-peptide nucleic acid conjugates》, the research content is summarized as follows. Peptide-Peptide Nucleic Acid (PNA) conjugates targeting essential bacterial genes have shown significant potential in developing novel antisense antimicrobials. The majority of efforts in this area are focused on identifying different PNA targets and the selection of peptides to deliver the peptide-PNA conjugates to Gram-neg. bacteria. Notably, the selection of a linkage strategy to form peptide-PNA conjugate plays an important role in the effective delivery of PNAs. Recently, a unique Cysteine- 2-Cyanoisonicotinamide (Cys- CINA) click chem. has been employed for the synthesis of cyclic peptides. Considering the high selectivity of this chem., we investigated the efficiency of Cys-CINA conjugation to synthesize novel antimicrobial peptide-PNA conjugates. The PNA targeting acyl carrier protein gene (acpP), when conjugated to the membrane-active antimicrobial peptides (polymyxin), showed improvement in antimicrobial activity against multidrug-resistant Gram-neg. Acinetobacter baumannii. Thus, indicating that the Cys-CINA conjugation is an effective strategy to link the antisense oligonucleotides with antimicrobial peptides. Therefore, the Cys-CINA conjugation opens an exciting prospect for antimicrobial drug development.

Nwajiobi, Ogonna team published research on Journal of the American Chemical Society in 2022 | 35737-15-6

Nwajiobi, Ogonna;Verma, Ashish Kumar;Raj, Monika research published 《 Rapid arene triazene chemistry for macrocyclization》, the research content is summarized as follows. Here, we report a novel rapid arene triazene strategy for the macrocyclization of peptides that generates an inbuilt chromophoric triazene moiety at the site of cyclization within a minute. The rapid arene triazene chem. is chemoselective for secondary amines and p-amino phenylalanine. Importantly, the resulting triazene cyclic peptide is highly stable at neutral pH and under harsh conditions but rapidly responds to various external stimuli such as UV radiations and acidic conditions, resulting in the ring opening to generate the linear peptides in an unchanged form, which further cyclizes under neutral pH conditions. This method works with completely unprotected peptides and has been applied for the synthesis of 18- to 66-membered monocycles and bicycles with various amino acid compositions in one pot under neutral pH conditions. Due to the high stability of triazene cyclic peptides, the postcyclization modification was carried out with various functional groups. This rapid, macrocyclization strategy featuring a triazene scaffold, amenable to late-stage diversification and responsive to external stimuli, should find application in various fields of chem. biol., selective drug delivery, and identification of cyclic peptide hits after library screening.

Mishra, Abhaya Kumar team published research on Angewandte Chemie, International Edition in 2021 | 35737-15-6

Mishra, Abhaya Kumar;Tessier, Romain;Hari, Durga Prasad;Waser, Jerome research published 《 Amphiphilic iodine(III) reagents for the lipophilization of peptides in water》, the research content is summarized as follows. We report the functionalization of cysteine residues with lipophilic alkynes bearing a silyl group or an alkyl chain using amphiphilic ethynylbenziodoxolone reagents (EBXs). The reactions were carried out in buffer (pH 6 to 9), without organic co-solvent or removal of oxygen, either at 37°C or room temperature The transformation led to a significant increase of peptide lipophilicity and worked for aromatic thiols, homocysteine, cysteine, and peptides containing 4 to 18 amino acids. His₆-Cys-Ubiquitin was also alkynylated under physiol. conditions. Under acidic conditions, the thioalkynes were converted into thioesters, which could be cleaved in the presence of hydroxylamine.

Mitra, Suchitra team published research on ACS Catalysis in 2021 | 35737-15-6

Mitra, Suchitra;Prakash, Divyansh;Rajabimoghadam, Khashayar;Wawrzak, Zdzislaw;Prasad, Pallavi;Wu, Tong;Misra, Sandeep K.;Sharp, Joshua S.;Garcia-Bosch, Isaac;Chakraborty, Saumen research published 《 De Novo Design of a Self-Assembled Artificial Copper Peptide that Activates and Reduces Peroxide》, the research content is summarized as follows. Copper-containing metalloenzymes constitute a major class of proteins that catalyze a myriad of reactions in nature. Inspired by the structural and functional characteristics of this unique class of metalloenzymes, we report the conception, design, characterization, and functional studies of a de novo artificial copper peptide (ArCuP) within a trimeric self-assembled polypeptide scaffold that activates and reduces peroxide. Using a first-principles approach, the ArCuP was designed to coordinate one Cu via three His residues introduced at an a site of the peptide scaffold. X-ray crystallog., UV-vis, and ESR data demonstrate that Cu binds via the N_ε atoms of His forming a T2Cu environment. When reacted with hydrogen peroxide, the putative copper-hydroperoxo species is formed where a reductive priming step accelerates the rate of its formation and reduction Mass spectrometry was used to identify specific residues undergoing oxidative modification, which showed His oxidation only in the reduced state. The redox behavior of the ArCuP was elucidated by protein film voltammetry. Detailed characterization of the electrocatalytic behavior of the ArCuP led us to determine the catalytic parameters (K_M and k_cat), which established the peroxidase activity of the ArCuP. Combined spectroscopic and electrochem. data showed a pH dependence on the reactivity, which was optimum at pH 7.5.

Modrzycka, Sylwia team published research on Chemical Science in 2022 | 35737-15-6

Recommanded Product: Fmoc-Trp-OH, Nalpha-FMOC-L-Tryptophan,also known as Fmoc-Trp-OH， is a useful research compound. Its molecular formula is C26H22N2O4 and its molecular weight is 426.5 g/mol. The purity is usually 95%.
Nα-Fmoc-L-Tryptophan is an N-Fmoc protected form of L-Tryptophan (T947210). L-Tryptophan is an essential amino acid that is important for cell proliferation and the biosynthesis of proteins. It is a precursor to Serotonin (HCl: S274980), a neurotransmitter that compound that aids in sleep and mental state. L-Tryptophan is also thought to cause eosinophilia-myalgia syndrome.
Fmoc-Trp-OH is an amino acid derivative
Fmoc-L-Trp-OH is an amide that contains a low bioavailability and inhibits the transfer of amino acids to ribosomes. It has been shown to inhibit the growth of cancer cells in cell culture and to have antimicrobial activity. Fmoc-L-Trp-OH is synthesized by reacting Naphthalene with glycine, followed by hydrolysis of the ester group under trifluoroacetic acid. The product is then conjugated with a polypeptide. This method of synthesis was developed as a way to produce peptides that are difficult to synthesize using solid-phase chemistry., 35737-15-6.

Modrzycka, Sylwia;Kolt, Sonia;Polderdijk, Stephanie G. I.;Adams, Ty E.;Potoczek, Stanislaw;Huntington, James A.;Kasperkiewicz, Paulina;Drag, Marcin research published 《 Parallel imaging of coagulation pathway proteases activated protein C, thrombin, and factor Xa in human plasma》, the research content is summarized as follows. Activated protein C (APC), thrombin, and factor (f) Xa are vitamin K-dependent serine proteases that are key factors in blood coagulation. Moreover, they play important roles in inflammation, apoptosis, fibrosis, angiogenesis, and viral infections. Abnormal activity of these coagulation factors has been related to multiple conditions, such as bleeding and thrombosis, Alzheimer′s disease, sepsis, multiple sclerosis, and COVID-19. The individual activities of APC, thrombin, and fXa in coagulation and in various diseases are difficult to establish since these proteases are related and have similar substrate preferences. Therefore, the development of selective chem. tools that enable imaging and discrimination between coagulation factors in biol. samples may provide better insight into their roles in various conditions and potentially aid in the establishment of novel diagnostic tests. In our study, we used a large collection of unnatural amino acids, and this enabled us to extensively explore the binding pockets of the enzymes′ active sites. Based on the specificity profiles obtained, we designed highly selective substrates, inhibitors, and fluorescent activity-based probes (ABPs) that were used for fast, direct, and simultaneous detection of APC, thrombin, and fXa in human plasma.

Molloy, Evelyn M. team published research on Angewandte Chemie, International Edition in 2021 | 35737-15-6

Molloy, Evelyn M.;Dell, Maria;Haensch, Veit G.;Dunbar, Kyle L.;Feldmann, Romy;Oberheide, Ansgar;Seyfarth, Lydia;Kumpfmueller, Jana;Horch, Therese;Arndt, Hans-Dieter;Hertweck, Christian research published 《 Enzyme-primed native chemical ligation produces autoinducing cyclopeptides in clostridia》, the research content is summarized as follows. Clostridia coordinate many important processes such as toxin production, infection, and survival by d.-dependent communication (quorum sensing) using autoinducing peptides (AIPs). Although clostridial AIPs have been proposed to be (thio)lactone-containing peptides, their true structures remain elusive. Here, we report the genome-guided discovery of an AIP that controls endospore formation in Ruminiclostridium cellulolyticum. Through a combination of chem. synthesis and chem. complementation assays with a mutant strain, we reveal that the genuine chem. mediator is a homodetic cyclopeptide (cAIP). Kinetic analyses indicate that the mature cAIP is produced via a cryptic thiolactone intermediate that undergoes a rapid S→N acyl shift, in a manner similar to intramol. native chem. ligation (NCL). Finally, by implementing a chem. probe in a targeted screen, we show that this novel enzyme-primed, intramol. NCL is a widespread feature of clostridial AIP biosynthesis.