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.
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 Nε 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 (KM and kcat), 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.
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.
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