35737-15-6 | - Page 9 of 10 - Indole Building Blocks

Fumagalli, Gabriele team published research on Journal of Medicinal Chemistry in 2021 | 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., Name: Fmoc-Trp-OH

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. Name: Fmoc-Trp-OH.

Fumagalli, Gabriele;Carbajo, Rodrigo J.;Nissink, J. Willem M.;Tart, Jonathan;Dou, Rongxuan;Thomas, Andrew P.;Spring, David R. research published 《 Targeting a novel KRAS binding site: Application of one-component stapling of small (5-6-mer) peptides》, the research content is summarized as follows. RAS proteins are central in the proliferation of many types of cancer, but a general approach toward the identification of pan-mutant RAS inhibitors has remained unresolved. In this work, we describe the application of a binding pharmacophore identified from anal. of known RAS binding peptides to the design of novel peptides. Using a chem. divergent approach, we generated a library of small stapled peptides from which we identified compounds with weak binding activity. Exploration of structure-activity relationships (SARs) and optimization of these early compounds led to low-micromolar binders of KRAS that block nucleotide exchange.

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

Fujiwara, Daisuke team published research on ChemBioChem in 2021 | 35737-15-6

COA of 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.

Indole, also called Benzopyrrole, a heterocyclic organic compound occurring in some flower oils, such as jasmine and orange blossom, in coal tar, and in fecal matter. 35737-15-6, formula is C26H22N2O4, Name is Fmoc-Trp-OH. It is used in perfumery and in making tryptophan, an essential amino acid, and indoleacetic acid (heteroauxin), a hormone that promotes the development of roots in plant cuttings. COA of Formula: C26H22N2O4.

Fujiwara, Daisuke;Mihara, Kousuke;Takayama, Ryo;Nakamura, Yusuke;Ueda, Mitsuhiro;Tsumuraya, Takeshi;Fujii, Ikuo research published 《 Chemical Modification of Phage-Displayed Helix-Loop-Helix Peptides to Construct Kinase-Focused Libraries》, the research content is summarized as follows. Conformationally constrained peptides hold promise as mol. tools in chem. biol. and as a new modality in drug discovery. The construction and screening of a target-focused library could be a promising approach for the generation of de novo ligands or inhibitors against target proteins. Here, we have prepared a protein kinase-focused library by chem. modifying helix-loop-helix (HLH) peptides displayed on phage and subsequently tethered to adenosine. The library was screened against aurora kinase A (AurA). The selected HLH peptide Bip-3 retained the α-helical structure and bound to AurA with a K_D value of 13.7 μM. Bip-3 and the adenosine-tethered peptide Bip-3-Adc provided IC₅₀ values of 103 μM and 7.7 μM, resp., suggesting that Bip-3-Adc bivalently inhibited AurA. In addition, the selectivity of Bip-3-Adc to several protein kinases was tested, and was highest against AurA. These results demonstrate that chem. modification can enable the construction of a kinase-focused library of phage-displayed HLH peptides.

Fowkes, Milan M. team published research on PLoS One in 2022 | 35737-15-6

Quality Control 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.

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). Quality Control of 35737-15-6.

Fowkes, Milan M.;Das Neves Borges, Patricia;Cacho-Nerin, Fernando;Brennan, Paul E.;Vincent, Tonia L.;Lim, Ngee H. research published 《 Imaging articular cartilage in osteoarthritis using targeted peptide radiocontrast agents》, the research content is summarized as follows. Established MRI and emerging X-ray contrast agents for non-invasive imaging of articular cartilage rely on non-selective electrostatic interactions with neg. charged proteoglycans. These contrast agents have limited prognostic utility in diseases such as osteoarthritis (OA) due to the characteristic high turnover of proteoglycans. To overcome this limitation, we developed a radiocontrast agent that targets the type II collagen macromol. in cartilage and used it to monitor disease progression in a murine model of OA. To confer radiopacity to cartilage contrast agents, the naturally occurring tyrosine derivative 3,5-diiodo-L-tyrosine (DIT) was introduced into a selective peptide for type II collagen. Synthetic DIT peptide derivatives were synthesized by Fmoc-based solid-phase peptide synthesis and binding to ex vivo mouse tibial cartilage evaluated by high-resolution micro-CT. Di-Iodotyrosinated Peptide Imaging of Cartilage (DIPIC) was performed ex vivo and in vivo 4, 8 and 12 wk in mice after induction of OA by destabilization of the medial meniscus (DMM). Finally, human osteochondral plugs were imaged ex vivo using DIPIC. Fifteen DIT peptides were synthesized and tested, yielding seven leads with varying cartilage binding strengths. DIPIC visualised ex vivo murine articular cartilage comparably to the ex vivo contrast agent phosphotungstic acid. Intra-articular injection of contrast agent followed by in vivo DIPIC enabled delineation of damaged murine articular cartilage. Finally, the translational potential of the contrast agent was confirmed by visualisation of ex vivo human cartilage explants. DIPIC has reduction and refinement implications in OA animal research and potential clin. translation to imaging human disease.

Duggan, Nisharnthi M. team published research on Organic Letters in 2021 | 35737-15-6

Duggan, Nisharnthi M.;Saez, Natalie J.;Clayton, Daniel;Budusan, Elena;Watson, Emma E.;Tucker, Isaac J.;Rash, Lachlan D.;King, Glenn F.;Payne, Richard J. research published 《 Total synthesis of the spider-venom peptide Hi1a》, the research content is summarized as follows. Hi1a is a venom peptide from the Australian funnel-web spider Hadronyche infensa with a complex tertiary structure. Hi1a has neuroprotective and cardioprotective properties due to its potent inhibition of acid-sensing ion channel 1a (ASIC1a) and is currently being pursued as a novel therapy for acute ischemic events. Herein, we describe the total synthesis of Hi1a using native chem. ligation. The synthetic peptide was successfully folded and exhibited similar inhibitory activity on ASIC1a to recombinant Hi1a.

Egelund, Peter H. G. team published research on ACS Sustainable Chemistry & Engineering in 2021 | 35737-15-6

Synthetic Route 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.

Egelund, Peter H. G.;Jadhav, Sandip;Martin, Vincent;Johansson Castro, Henrik;Richner, Franziska;Le Quement, Sebastian Thordal;Dettner, Frank;Lechner, Carolin;Schoenleber, Ralph;Sejer Pedersen, Daniel research published 《 Fmoc-removal with pyrrolidine expands the available solvent space in green solid-phase peptide synthesis》, the research content is summarized as follows. Green binary solvent mixtures with a polarity and viscosity close to that of DMF perform similarly in solid-phase peptide synthesis (SPPS). However, while coupling reactions readily proceed in solvents of significantly lower polarity than that of DMF, a high solvent polarity is essential for Fmoc-removal (Fmoc = 9-fluorenylmethoxycarbonyl) using piperidine, which limits the options for green SPPS solvents. Herein, we report our efforts to expand the available solvent polarity space for green SPPS. We identified pyrrolidine as an efficient base to enable Fmoc-removal in less polar solvent mixtures that also favor coupling reactions, such as DMSO/ethyl acetate (1:9) and N-butylpyrrolidone/1,3-dioxolane (2:8 and 4:6). Employing less polar binary solvent mixtures in combination with pyrrolidine gave crude peptide purities comparable to or better than for DMF with piperidine in the SPPS of challenging peptide targets. An evaluation of base-dependent side reactions such as diketopiperazine (DKP) and aspartimide formation showed increased side-product formation when using pyrrolidine on DKP- and aspartimide-prone sequences. However, the scaled-up syntheses (5 and 7.5 mmol, resp.) of the peptide therapeutics dasiglucagon (29-mer) and bivalirudin (20-mer) gave good crude peptide purities and purity profiles amenable to SPPS optimization. Pyrrolidine therefore represents a useful alternative to piperidine for Fmoc-removal in an expanded solvent space for green SPPS.

Elkhalifa, Mahmoud team published research on Organic Letters 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.

Elkhalifa, Mahmoud;Elbaum, Michael B.;Chenoweth, David M.;Molander, Gary A. research published 《 Solid-phase photochemical decarboxylative hydroalkylation of peptides》, the research content is summarized as follows. The compatibility of photochem. with solid-phase peptide synthesis is demonstrated via photochem. hydroalkylation to form C(sp³)-C(sp³) bonds between on-resin Giese acceptors and redox-active esters. Both iridium-based photocatalysts and Hantszch ester led to high yields, with final reaction conditions producing full conversions within 30 min under ambient conditions. The chem. is compatible with a broad range of peptide side chains, redox-active esters, and resin. These conditions represent the first example of photochem. peptide modifications on resin.

Drayton, Matthew team published research on Journal of Controlled Release in 2021 | 35737-15-6

Drayton, Matthew;Alford, Morgan A.;Pletzer, Daniel;Haney, Evan F.;Machado, Yoan;Luo, Haiming D.;Overall, Christopher M.;Kizhakkedathu, Jayachandran N.;Hancock, Robert E. W.;Straus, Suzana K. research published 《 Enzymatically releasable polyethylene glycol – host defense peptide conjugates with improved activity and biocompatibility》, the research content is summarized as follows. Host defense peptides (HDPs) have been the subject of great interest for the treatment of multidrug-resistant bacterial infections due to their multimodal activity and low induction of resistance. However, aggregation, toxicity, and short biol. half-life have limited their applicability for clin. treatment. Many methods have been explored to alleviate these issues, such as polymer (e.g., polyethylene glycol (PEG)) conjugation, but these are often accompanied by reductions in the activity of the HDP. Here, we detail the design of a novel PEG-HDP conjugate incorporating an enzymic cleavage sequence targeting matrix metalloproteinases (MMPs) that accumulate at sites of inflammation and infection. Addition of the cleavage sequence onto either the N- or the C-terminal region of the parent peptide (peptide 73, a derivative of the HDP aurein 2.2) was explored to determine the location for optimal antimicrobial activity following MMP cleavage; furthermore, the susceptibility of the peptide to MMP cleavage after conjugation to 2 kDa or 5 kDa PEG was examined The top candidate, L73, utilized an N-terminal cleavage site that was subsequently conjugated to a 2 kDa PEG polymer. Both L73 and the conjugate exhibited no antimicrobial activity in vitro until cleaved by purified MMP, which liberated a peptide fragment with 16- or 63-fold improved activity, resp., corresponding to a min. inhibitory concentration (MIC) of 8 μg/mL, comparable to that of peptide 73 (4 μg/mL). Furthermore, PEG conjugation improved the blood compatibility and reduced the aggregation tendency of the HDP in vitro, indicating enhanced biocompatibility. When administered as a single s.c. dose (∼3.6 mg, or a peptide concentration of 142 mg/kg) in a mouse abscess model of high-d. methicillin-resistant Staphylococcus aureus (MRSA) infection, the conjugate displayed strong activity, reducing abscess size and bacterial load by 73.3% and 58-fold, resp. This activity was completely lost when the cleavage site was rendered resistant to MMPs by the substitution of two D-amino acids, supporting the hypothesis that antimicrobial activity was dependent on cleavage by MMPs, which were shown here to increasingly accumulate at the abscess site up to 18 h post infection. Finally, the conjugate displayed biocompatibility in vivo, with no identifiable toxicity or aggregation.

Depuydt, Anne-Sophie team published research on ACS Pharmacology & Translational Science in 2021 | 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. SDS of cas: 35737-15-6.

Depuydt, Anne-Sophie;Rihon, Jerome;Cheneval, Olivier;Vanmeert, Michiel;Schroeder, Christina I.;Craik, David J.;Lescrinier, Eveline;Peigneur, Steve;Tytgat, Jan research published 《 Cyclic Peptides as T-Type Calcium Channel Blockers: Characterization and Molecular Mapping of the Binding Site》, the research content is summarized as follows. T-type calcium (Ca_V3) channels play a crucial role in the generation and propagation of action potentials in excitable cells and are considered potential drug targets for the treatment of neurol. and cardiovascular diseases. Given the limited pharmacol. repertoire for these channels, there is a great need for novel potent and selective Ca_V3 channel inhibitors. In this study, we used Xenopus oocytes to heterologously express Ca_V3.1 channels and characterized the interaction with a small cyclic peptide, PnCS1. Using mol. modeling, PnCS1 was docked into the cryo-electron microscopy structure of the human Ca_V3.1 channel and mol. dynamics were performed on the resultant complex. The binding site of the peptide was mapped with the involvement of critical amino acids located in the pore region and fenestrations of the channel. More specifically, we found that PnCS1 reclines in the central cavity of the pore domain of the Ca_V3.1 channel and resides stably between the selectivity filter and the intracellular gate, blocking the conduction pathway of the channel. Using Multiple Attribute Positional Scanning approaches, we developed a series of PnCS1 analogs. These analogs had a reduced level of inhibition, confirming the importance of specific residues and corroborating our modeling. In summary, functional studies of PnCS1 on the Ca_V3.1 channel combined with mol. dynamics results provide the basis for understanding the mol. interactions of PnCS1 with Ca_V3.1 and are fundamental to structure-based drug discovery for treating Ca_V3 channelopathies.

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

Deng, Xingwang;Zhou, Guan;Tian, Jing;Srinivasan, Rajavel research published 《 Chemoselective Amide-Forming Ligation Between Acylsilanes and Hydroxylamines Under Aqueous Conditions》, the research content is summarized as follows. We report the facile amide-forming ligation of acylsilanes R¹COSiMe₃ with hydroxylamines R²NHOCONEt₂ (ASHA ligation) under aqueous conditions, yielding amides R¹CONHR² in a chemoselective way in MeCN/H₂O mixtures catalyzed by citric acid. The ligation is fast, chemoselective, mild, high-yielding and displays excellent functional-group tolerance. Late-stage modifications of an array of marketed drugs, peptides, natural products, and biol. active compounds showcase the robustness and functional-group tolerance of the reaction. The key to the success of the reaction could be the possible formation of the strong Si-O bond via a Brook-type rearrangement. Given its simplicity and efficiency, this ligation has the potential to unfold new applications in the areas of medicinal chem. and chem. biol.

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

Dai, Shijie;Hong, Haofei;Zhou, Kun;Zhao, Kai;Xie, Yuntian;Li, Chen;Shi, Jie;Zhou, Zhifang;Nie, Lei;Wu, Zhimeng research published 《 Exendin 4-Hapten Conjugate Capable of Binding with Endogenous Antibodies for Peptide Half-life Extension and Exerting Long-Acting Hypoglycemic Activity》, the research content is summarized as follows. Hapten-specific endogenous antibodies are naturally occurring antibodies present in human blood. Herein, we investigated a new strategy in which small-mol. haptens were utilized as naturally occurring antibody binders for peptide half-life extension. The glucagon-like peptide 1 receptor agonist exendin 4 was site-specifically functionalized with the dinitrophenyl (DNP) hapten at the C-terminus via sortase A-mediated ligation. The resulting Ex4-DNP conjugates retained GLP-1 receptor activation potency in vitro and had a similar in vivo acute glucose-lowering effect comparable to that of native Ex4. Pharmacokinetic studies and hypoglycemic duration tests demonstrated that the Ex4-DNP conjugates displayed significantly elongated half-lives and improved long-acting antidiabetic activity in the presence of endogenous anti-DNP antibodies. In chronic treatment studies, once-daily administration of optimal conjugate 7 demonstrated more beneficial effects without prominent toxicity compared with Ex4. This strategy provides a new approach and represents an alternative to the well-established peptide-Fc fusion strategy to improve the peptide half-life and the therapeutic efficacy.