35737-15-6 | - Indole Building Blocks

Zhu, Han-Ying team published research on Tetrahedron Letters 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, 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. Electric Literature of 35737-15-6.

Zhu, Han-Ying;Wu, Meng;Yu, Fei-Qiang;Zhang, Yan-Ni;Xi, Tong-Kuai;Chen, Kai;Fang, Ge-Min research published 《 Chemical synthesis of thioether-bonded bicyclic peptides using tert-butylthio and Trt-protected cysteines》, the research content is summarized as follows. Thioether-bonded bicyclic peptide can resist proteolytic degradation and become a promising scaffold for peptide-based inhibitor discovery. Chem. synthesis of thioether-bonded bicyclic peptide usually requires two orthogonal Cys protecting groups. Here, we report an efficient strategy for its preparation by using the commonly used Trt-protected and StBu-protected cysteines. Due to the thiol-disulfide exchange, S-StBu group is generally considered incompatible with sulfhydryl group under neutral conditions. We find that, in DIPEA-containing DMF solution, the peptide that contains both sulfhydryl and S-StBu groups can undergo selective thiol bisalkylation while maintaining the integrity of the S-StBu groups. In our strategy, the formation of two thioether bonds are both conducted in solution, and can be easily tracked by HPLC, which may be beneficial for the chem. synthesis of thioether-bonded bicyclic peptides.

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

Zhao, Liang team published research on Advanced Healthcare Materials in 2022 | 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.

Zhao, Liang;Chen, Junyi;Tian, Long;Zhang, Yahan;Chen, Longming;Du, Xinbei;Ma, Mengke;Li, Jian;Meng, Qingbin;Li, Chunju research published 《 Supramolecular Detoxification of Macromolecular Biotoxin through the Complexation by a Large-Sized Macrocycle》, the research content is summarized as follows. Biotoxins are diverse, complex, and hypertoxic, ultimately serving as grave and lasting menaces to humanity. Here, it is aimed to introduce a new detoxification methodol. for macromol. biotoxin through complexation by a very large macrocycle. A 25-mer peptide isolated from Lycosa erythrognatha spider venom (LyeTxI) is selected as the model macromol. biotoxin. Quaterphen[4]arene, with a side length of ≈1.6 nm, has a sufficient cavity to bind LyeTxI. Hence, the water-soluble derivative of Quaterphen[4]arene (H) is designed and synthesized. H exhibits an overall host-guest complexation toward LyeTxI, resulting in a considerably high association constant of (7.01 ± 0.18) x 10⁷ M^-1. This encapsulation of peptide is interesting as traditional macrocycles can only engulf the amino acid residues of peptides due to their limited cavity size. In vitro assay verifies that complexation by H inhibits the interactions of LyeTxI with cell membranes, thereby reducing its cytotoxicity, suppressing hemolysis, and decreasing the release of lactate dehydrogenase. Notably, the i.v. administration of H has a significant therapeutic effect on LyeTxI-poisoned mice, alleviating inflammation and tissue damage, and markedly improving the survival rate from 10% to 80%. An efficient and potentially versatile approach is provided to detoxify macromol. biotoxins, with giant macrocycle serving as an antidote.

Yum, Ji Hye team published research on ACS Biomaterials Science & Engineering in 2021 | 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.

Yuan, Zhenbo team published research on Green Chemistry 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

Yuan, Zhenbo;Lu, Liushen;Liu, Meiling;Liu, Xuanzhong;Liu, Changmei;Yin, Dejing;Zhang, Yan;Rao, Yijian research published 《 Natural product cercosporin as a bioinspired photocatalyst for the synthesis of peptides containing kynurenine via an energy transfer mechanism》, the research content is summarized as follows. Cercosporin-catalyzed photo-mediated oxidation for the rapid and efficient synthesis of kynurenine (Kyn) derivatives as well as Kyn-containing peptides under mild conditions was developed, exhibiting great functional group tolerance and broad substrate scope to produce various nonproteinogenic peptides. This environmentally friendly process utilized the natural product cercosporin (CP) as a metal-free photocatalyst, visible light as a sustainable energy source, and oxygen as a green oxidant. Moreover, the synthetic utility of this photooxidation reaction was exemplified by the gram-scale synthesis employing crude CP conveniently obtained from the fermentation broth of Cercospora, and the successive transformation to kynurenine. Finally, preliminary mechanistic studies revealed that an energy transfer pathway was involved in the reaction.

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

Yin, Huawu;Zhou, Xiuman;Huang, Yen-Hua;King, Gordon J.;Collins, Brett M.;Gao, Yanfeng;Craik, David J.;Wang, Conan K. research published 《 Rational Design of Potent Peptide Inhibitors of the PD-1:PD-L1 Interaction for Cancer Immunotherapy》, the research content is summarized as follows. Peptides have potential to be developed into immune checkpoint inhibitors, but the target interfaces are difficult to inhibit. Here, we explored an approach to mimic the binding surface of PD-1 to design inhibitors. Mimicking native PD-1 resulted in a mimetic with no activity. However, mimicking an affinity-optimized PD-1 resulted in the peptide mimetic MOPD-1 that displayed nanomolar affinity to PD-L1 and could inhibit PD-1:PD-L1 interactions in both protein- and cell-based assays. Mutagenesis and structural characterization using NMR spectroscopy and X-ray crystallog. revealed that binding residues from the high affinity PD-1 are crucial for the bioactivity of MOPD-1. Furthermore, MOPD-1 was extremely stable in human serum and inhibited tumor growth in vivo, suggesting it has potential for use in cancer immunotherapy. The successful design of an inhibitor of PD-1:PD-L1 using the mimicry approach described herein illustrates the value of placing greater emphasis on optimizing the target interface before inhibitor design and is an approach that could have broader utility for the design of peptide inhibitors for other complex protein-protein interactions.

Yao, Guiyang team published research on Journal of the American Chemical Society in 2021 | 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. Computed Properties of 35737-15-6.

Yao, Guiyang;Knittel, Caroline H.;Kosol, Simone;Wenz, Marius T.;Keller, Bettina G.;Gruss, Hendrik;Braun, Alexandra C.;Lutz, Christian;Hechler, Torsten;Pahl, Andreas;Suessmuth, Roderich D. research published 《 Iodine-mediated tryptathionine formation facilitates the synthesis of amanitins》, the research content is summarized as follows. Synthetic methods on the macrocyclization of peptides are of high interest since they facilitate the synthesis of various types of potentially bioactive compounds, e.g. addressing targets like protein-protein-interactions. Herein, we report on an efficient method to construct tryptathionine-cross-links in peptides between the amino acids Trp and Cys. This reaction not only is the basis for the total synthesis of the death cap toxin α-amanitin but also provides rapid access to various new amanitin analogs. This study for the first time presents a systematic compilation of structure-activity relations (SAR) of amatoxins with regard to RNA polymerase II inhibition and cytotoxicity with one amanitin derivative of superior RNAP II inhibition. The present approach paves the way for the synthesis of structurally diverse amatoxins as future payloads for antibody-toxin conjugates in cancer therapy.

Yang, Yi team published research on Organic Process Research & Development in 2021 | 35737-15-6

Safety of 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.

Yang, Yi;Hansen, Lena;Fraczek, Aleksandra;Badalassi, Fabrizio;Kjellstrom, Johan research published 《 DMF-assisted iodination side reaction during the preparation of disulfide peptides, its substrate/solvent/Ph dependence, and implications on disulfide-peptide production》, the research content is summarized as follows. Severe iodination of a disulfide peptide mol. (peptide D) was detected from the on-resin disulfide cyclization process. LC/MS/MS results indicated that iodination occurred on the Thi (thienylalanine) residue. Systematic investigation revealed that the iodination reaction occurred predominantly in the I₂/DMF-mediated on-resin disulfide formation reaction. The iodination side reaction was strongly solvent-dependent and favored in DMF and NMP. A tentative mechanism similar to that of the Vilsmeier-Haack reaction was proposed. A variety of amino acid/peptide substrates were tested as iodination substrates. The results indicated the susceptibility of amino acids with electron-rich aromatic groups to iodination. Addnl., various solutions were proposed for preventing peptide iodination based on the findings in this study. This study demonstrates the applicability of the on-resin disulfide production of peptides bearing electron-rich aromatic residues.

Yang, Su team published research on ChemBioChem in 2021 | 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.

Yang, Su;Chang, Yan;Hazoor, Shan;Brautigam, Chad;Foss, Frank W. Jr.;Pan, Zui;Dong, He research published 《 Modular Design of Supramolecular Ionic Peptides with Cell-Selective Membrane Activity》, the research content is summarized as follows. The rational design of materials with cell-selective membrane activity is an effective strategy for the development of targeted mol. imaging and therapy. Here we report a new class of cationic multidomain peptides (MDPs) that can undergo enzyme-mediated mol. transformation followed by supramol. assembly to form nanofibers in which cationic clusters are presented on a rigid β-sheet backbone. This structural transformation, which is induced by cells overexpressing the specific enzymes, led to a shift in the membrane perturbation potential of the MDPs, and consequently enhanced cell uptake and drug delivery efficacy. We envision the directed self-assembly based on modularly designed MDPs as a highly promising approach to generate dynamic supramol. nanomaterials with emerging membrane activity for a range of disease targeted mol. imaging and therapy applications.

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.

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.

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.