103321-54-6Relevant articles and documents
Eco-friendly synthesis of peptides using fmoc-amino acid chlorides as coupling agent under biphasic condition
Kantharaju, Kamanna,Khatavi, Santosh Y.
, p. 699 - 707 (2021/08/23)
Background: Agro-waste derived solvent media act as a greener process for the peptide bond formation using Nα-Fmoc-amino acid chloride and amino acid ester salt with in situ neutralization and coupling under biphasic condition. The Fmoc-amino acid chlorides are prepared by the reported procedure of freshly distilled SOCl2 with dry CH2Cl2. The protocol found many added ad-vantages such as neutralization of amino acid ester salt and not required additional base for the neu-tralization, and directly coupling take place with Fmoc-amino acid chloride gave final product dipeptide ester in good to excellent yields. The protocol occurs with complete stereo chemical integrity of the configuration of substrates. Here, we revisited Schotten-Baumann condition, instead of using inorganic base. Objective: To develop green protocol for the synthesis of peptide bond using Fmoc-amino acid chloride with amino acid esters salt. Methods: The final product isolated is analyzed in several spectroscopic and analytical techniques such as FT-IR,1H-,13C-NMR, Mass spectrometry and RP-HPLC to check stereo integrity and puri-ty of the product. Conclusion: The present method developed greener using natural agro-waste (lemon fruit shell ash) derived solvent medium for the reaction and not required chemical entity.
Preparation method of methionine derivative corrosion inhibitor
-
, (2016/10/31)
The invention discloses a preparation method of a methionine derivative corrosion inhibitor. The method comprises the following steps: synthesis of Fmoc-methionine: adding methionine and Fmoc-OSu into a DMF (N,N-dimethylformamide) solvent to react, and adding NaHCO3 to remove the solvent and residual amine compounds, thereby obtaining the product, wherein the yield is 78%; synthesis of Fmoc-methionine acyl chloride: adding the Fmoc-methionine into 25ml of CH2Cl2, and refluxing to react for 4 hours; and synthesis of Fmoc-methionine amide: after the acyl-chlorination reaction, directly adding into an equal mole of octadecylamine CH2Cl2 solution to obtain a yellow solid, and purifying the product by a chromatographic column separation process, wherein the eluting solution is composed of dichloromethane and methanol in a volume ratio of 20:1. According to the preparation method, the Fmoc- protective group is connected to the methionine molecule by amidation, and the adsorption site formed by the pi-electron-containing benzene ring enhances the adsorptivity of the corrosion inhibitor molecule. The hydrophobic long chain is connected to the methionine molecule to resist the attack of water molecules, so that a protective film is formed on the steel surface, thereby achieving the goal of corrosion inhibition.
Benzotriazole-assisted solid-phase assembly of Leu-Enkephalin, amyloid β segment 34-42, and other "difficult" peptide sequences
Katritzky, Alan R.,Haase, Danniebelle N.,Johnsons, Jodie V.,Chung, Alfred
body text, p. 2028 - 2032 (2009/08/07)
Microwave-assisted solid-phase syntheses of six "difficult" peptides, H-VVSVV-NH2 (3), H-VVVSVV-NH2(4), H-VIVIG-OH (5), H-TVTVTV-NH2 (6), H-VKDGYI-NH2 (7), and H-VKDVYI-NH2 (8), were achieved utilizing N-(Fmoc-α-aminoacyl) benzotriazoles. Extension to the syntheses of Leu-enkephalin (9) and amyloid-β (34-42) (10) demonstrates that this strategy comprises an efficient route to new and known "difficult" peptides.
