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 (CaV3) 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 CaV3 channel inhibitors. In this study, we used Xenopus oocytes to heterologously express CaV3.1 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 CaV3.1 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 CaV3.1 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 CaV3.1 channel combined with mol. dynamics results provide the basis for understanding the mol. interactions of PnCS1 with CaV3.1 and are fundamental to structure-based drug discovery for treating CaV3 channelopathies.
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
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