M.W=400-450 | - Page 4 of 13 - Indole Building Blocks

Yum, Ji Hye team published research on ACS Biomaterials Science & Engineering in 2021 | 35737-15-6

Electric Literature 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). Electric Literature of 35737-15-6.

Yum, Ji Hye;Ishizuka, Takumi;Fukumoto, Koyuki;Hori, Daisuke;Bao, Hong-Liang;Xu, Yan;Sugiyama, Hiroshi;Park, Soyoung research published 《 Systematic Approach to DNA Aptamer Design Using Amino Acid-Nucleic Acid Hybrids (ANHs) Targeting Thrombin》, the research content is summarized as follows. Chem. modifications of innate DNA/RNA aptamers facilitate the improvement of their function. Herein, we report our modular strategy to manipulate a thrombin-binding DNA aptamer (TBA) to improve its anticoagulation activity and binding affinity. A set of amino acid conjugates, termed amino acid-nucleic acid hybrids or ANHs, was synthesized and incorporated into a TBA loop sequences. We found that substitutions with hydrophobic amino acids in the loop region possessed significantly enhanced antithrombin activity, up to 3-fold higher than the native TBA. We investigated the correlations between thrombin-binding affinity and the features of our amino-acid conjugates using exptl. techniques including CD spectroscopy, surface plasmon resonance assay, and mol. modeling. The present study demonstrates a systematic approach to aptamer design based on amino-acid characteristics, allowing the development of advanced aptamers.

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

Volpina, Olga M. team published research on Drug Development Research in 2021 | 35737-15-6

Application In Synthesis 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.

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. Application In Synthesis of 35737-15-6.

Volpina, Olga M.;Koroev, Dmitriy O.;Serebryakova, Marina V.;Volkova, Tatyana D.;Kamynina, Anna V.;Bobkova, Natalia V. research published 《 Proteolytic degradation patterns of the receptor for advanced glycation end products peptide fragments correlate with their neuroprotective activity in Alzheimer’s disease models》, the research content is summarized as follows. The receptor for advanced glycation end products (RAGE) plays an essential role in Alzheimer’s disease (AD). We previously demonstrated that a fragment (60-76) of RAGE improved the memory of olfactory bulbectomized (OBX) and Tg 5 x FAD mice – animal models of AD. The peptide analog (60-76) with protected N- and C-terminal groups was more active than the free peptide in Tg 5 x FAD mice. This study investigated proteolytic cleavage of the RAGE fragment (60-76) and its C- and N-terminally modified analog by blood serum using HPLC and mass spectrometry. The modified peptide was proteolyzed slower than the free peptide. Degrading the protected analog resulted in shortened fragments with memory-enhancing effects, whereas the free peptide yielded inactive fragments. After administering the different peptides to OBX mice, their performance in a spatial memory task revealed that the ED of the modified peptide was five times lower than that of the free peptide. HPLC and mass spectrometry anal. of the proteolytic products allowed us to clarify the differences in the neuroprotective activity conferred by administering these two peptides to AD animal models. The current study suggests that the modified RAGE fragment is more promising for the development of anti-AD therapy than its free analog.

Wang, Pengxin team published research on Organic Letters in 2021 | 35737-15-6

Reference 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, 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. Reference of 35737-15-6.

Wang, Pengxin;Cheng, Yulian;Wu, Chunlei;Zhou, Yimin;Cheng, Zhehong;Li, Hongchang;Wang, Rui;Su, Wu;Fang, Lijing research published 《 Tyrosine-specific modification via a dearomatization-rearomatization strategy: Access to azobenzene functionalized peptides》, the research content is summarized as follows. Azobenzene functionalized peptides are of great importance in photoresponsive biosystems and photopharmacol. Herein, we report an efficient approach to prepare azobenzene functionalized peptides through late-stage modification of tyrosine-containing peptides using a dearomatization-rearomatization strategy. This approach shows good chemoselectivity and site selectivity as well as sensitive group tolerance to various peptides. This method enriches the postsynthetic modification toolbox of peptides and has great potential to be applied in medicinal chem. and chem. biol.

Wang, Siyao team published research on Angewandte Chemie, International Edition 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., Category: indole-building-block

Wang, Siyao;Zhou, QingQing;Zhang, Xiaheng;Wang, Ping research published 《 Site-selective itaconation of complex peptides by photoredox catalysis》, the research content is summarized as follows. Site-selective peptide functionalization provides a straightforward and cost-effective access to diversify peptides for biol. studies. Among many existing non-invasive peptide conjugations methodologies, photoredox catalysis has emerged as one of the powerful approaches for site-specific manipulation on native peptides. Herein, we report a highly N-termini-specific method to rapidly access itaconated peptides and their derivatives through a combination of transamination and photoredox conditions. This strategy exploits the facile reactivity of peptidyl-dihydropyridine in the complex peptide settings, complementing existing approaches for bioconjugations with excellent selectivity under mild conditions. Distinct from conventional methods, this method utilizes the highly reactive carbamoyl radical derived from a peptidyl-dihydropyridine. In addition, this itaconated peptide can be further functionalized as a Michael acceptor to access the corresponding peptide-protein conjugate.

Wang, Zhengning team published research on Journal of the American Chemical Society in 2021 | 35737-15-6

Product Details of 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.

Wang, Zhengning;Wang, Xuewei;Wang, Penghui;Zhao, Junfeng research published 《 Allenone-mediated racemization/epimerization-free peptide bond formation and its application in peptide synthesis》, the research content is summarized as follows. Allenone has been identified as a highly effective peptide coupling reagent for the first time. The peptide bond was formed with an α-carbonyl vinyl ester as the key intermediate, the formation and subsequent aminolysis of which proceed spontaneously in a racemization-/epimerization-free manner. The allenone coupling reagent not only is effective for the synthesis of simple amides and dipeptides but is also amenable to peptide fragment condensation and solid-phase peptide synthesis (SPPS). The robustness of the allenone-mediated peptide bond formation was showcased incisively by the synthesis of carfilzomib, which involved a rare racemization-/epimerization-free N to C peptide elongation strategy. Furthermore, the successful synthesis of the model difficult peptide ACP (65-74) on a solid support suggested that this method was compatible with SPPS. This method combines the advantages of conventional active esters and coupling reagents, while overcoming the disadvantages of both strategies. Thus, this allenone-mediated peptide bond formation strategy represents a disruptive innovation in peptide synthesis.

Wang, Zhuoer team published research on Chinese Chemical Letters in 2021 | 35737-15-6

Wang, Zhuoer;Hao, Aiyou;Xing, Pengyao research published 《 Helical secondary structures and supramolecular tilted chirality in N-terminal aryl amino acids with diversified optical activities》, the research content is summarized as follows. Helix structures at at./mol. level have not been found in self-assembled peptide sequence with less than three residues. As β-sheet supramol. secondary structures have been discovered in solid-state amino acids, we here report the conjugation of simple N-terminal aryl protecting group could give rise to helical supramol. secondary structures in solid-state, which determines the optical activities of the adjacent aryl groups. The carboxylic acid-involved asym. H-bonds in N-terminal aryl amino acids induce the emergence of super-helical structures of amino acid residues and aryl groups. In most cases, supramol. tilted chirality of aryl groups is opposite to that of amino acid sequences, of which handedness and helical pitch are determined by the H-bond modalities. Determining correlation between supramol. tilted chirality of aryl segments and their chiroptical activities is firstly unveiled, which was verified by the computational results based on d. functional theory. Most aryl amino acids self-assembled by nanopptn. method via crystallization induced self-assembly into rigid one-dimensional microstructures with ultra-high Young’s modulus. This study reveals the generic existence of chiral supramol. structures in aggregated amino acid derivatives and gives an in-depth investigation into the structural-property relationships, which could guide the rational design and screening of chiroptical supramol. materials.

Wolf, Philipp team published research on Journal of Peptide Science in 2021 | 35737-15-6

Wolf, Philipp;Beck-Sickinger, Annette G. research published 《 The ring size of monocyclic ET-1 controls selectivity and signaling efficiency at both endothelin receptor subtypes》, the research content is summarized as follows. Cardiovascular diseases (CVDs) like hypertension are a major cause for death worldwide. In the cardiovascular tissue, the endothelin system-consisting of the receptor subtypes A (ET_AR) and B (ET_BR) and the mixed agonist endothelin 1 (ET-1)-is a major key player in the regulation of vascular tone and blood pressure. Tight control of this system is required to maintain homeostasis; otherwise, the endothelin system can cause severe CVDs like pulmonary artery hypertension. The high sequence homol. between both receptor subtypes limits the development of novel and selective ligands. Identification of small differences in receptor-ligand interactions and determination of selectivity constraints are crucial to fine-tune ligand properties and subsequent signaling events. Here, we report on novel ET-1 analogs and their detailed pharmacol. characterization. We generated simplified ET-1-derived monocyclic peptides to provide an accessible synthesis route. By detailed in vitro characterization, we demonstrated that both G protein signaling and the subsequent arrestin recruitment of activated ET_BR remain intact, whereas activation of the ET_AR depends on the intramol. ring size. Increasing of the intramol. ring structure reduces activity at the ET_AR and shifts the peptide toward ET_BR selectivity. All ET-1 analogs displayed efficient ET_BR-mediated signaling by G protein activation and arrestin 3 recruitment. Our study provides in-depth characterization of the ET-1/ET_AR and ET-1/ET_BR interactions, which has the potential for future development of endothelin-based drugs for CVD treatment. By identification of Lys⁹ for selective labeling, novel analogs for peptide-mediated shuttling by ET-1 are proposed.

Wu, Yaqi team published research on Bioconjugate Chemistry in 2021 | 35737-15-6

Wu, Yaqi;Li, Cong;Fan, Shihui;Zhao, Yibing;Wu, Chuanliu research published 《 Fast and selective reaction of 2-benzylacrylaldehyde with 1,2-aminothiol for stable N-terminal cysteine modification and peptide cyclization》, the research content is summarized as follows. N-terminal cysteine (Cys)-specific reactions have been exploited for protein and peptide modifications. However, existing reactions for N-terminal Cys suffer from low reaction rate, unavoidable side reactions, or poor stability for reagents or products. Herein we report a fast, efficient, and selective conjugation between 2-benzylacrylaldehyde (BAA) and 1,2-aminothiol, which involves multistep reactions including aldimine condensation, Michael addition, and reduction of imine by NaBH₃CN. This conjugation proceeds with a rate constant of ~2700 M^-1 s^-1 under neutral condition at room temperature to produce a pair of seven-membered ring diastereoisomers, which are stable under neutral and acidic conditions. This method enables the selective modifications of the N-terminal Cys residue without interference from the internal Cys and lysine residues, providing a useful alternative to existing approaches for site-specific peptide or protein modifications and synthesis of cyclic peptides.

Wu, Ye team published research on Chinese Chemical Letters 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.

Wu, Ye;Zou, Yan;Sun, Lingling;Garzino-Demo, Alfredo;Hu, Honggang;Zhang, Weidong;Li, Xiang research published 《 Peptide stapling with the retention of double native side-chains》, the research content is summarized as follows. All-hydrocarbon stapling strategy has been widely applied for enhancing the proteolytic stability of peptides. However, two major tech. hurdles to some extent limit the development of stapled peptides for therapeutic usage: rational selection of the stapling sites and the corresponding deletion of the native side chains. Previously we described the development of the olefin-terminated amino acids with the retention of native side chains and successfully applied them in the synthesis of hydrocarbon stapled peptides with single side-chain retention. Here, we explored the feasibility and effectiveness of hydrocarbon stapling strategy characterized as double side-chains retention. Modeled after a lengthy human immunodeficiency virus-1 (HIV-1) fusion inhibitor SC34EK, Leuⁱ, Serⁱ⁺⁴ and Lysⁱ, Leuⁱ⁺⁴ stapled peptides with the retention of double side-chains were effectively obtained. Our complementary study provided a convenient alternative to address where to install the staple in sequence for conventional all-hydrocarbon peptide stapling. Furthermore, this method not only conferred conformational reinforcement for SC34EK with high α-helicity and protease resistance, but also preserved the structural characteristic (key peripheral residues, charge and solubility) of the linear peptide to the maximum, which are crucial for anti-HIV-1 activity.

Takayama, Kentaro team published research on ACS Medicinal Chemistry Letters in 2022 | 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.

Takayama, Kentaro;Hitachi, Keisuke;Okamoto, Hideyuki;Saitoh, Mariko;Odagiri, Miki;Ohfusa, Rina;Shimada, Takahiro;Taguchi, Akihiro;Taniguchi, Atsuhiko;Tsuchida, Kunihiro;Hayashi, Yoshio research published 《 Development of Myostatin Inhibitory D-Peptides to Enhance the Potency, Increasing Skeletal Muscle Mass in Mice》, the research content is summarized as follows. Myostatin is a key neg. regulator of skeletal muscle growth, and myostatin inhibitors are attractive tools for the treatment of muscular atrophy. Previously, we reported a series of 14-29 mer peptide myostatin inhibitors, including a potent derivative MIPE-1686, a 16-mer N-terminal-free L-peptide with three unnatural amino acids and a propensity to form β-sheets. However, the biol. stability in vivo of MIPE-1686 is a concern for its development as a drug. In the present study, to develop a more stable myostatin inhibitory D-peptide (MID), various retro-inverso versions of a 16-mer peptide were synthesized. Among these, an arginine-containing derivative, MID-35 shows a potent and equivalent in vitro myostatin inhibitory activity equivalent to that of MIPE-1686 and considerable stability against biodegradation The in vivo potency of MID-35 to increase tibialis anterior muscle mass in mice is significantly enhanced over that of MIPE-1686 and MID-35 can serve as a new entity for the prolonged inactivation of myostatin in skeletal muscle.