Synthesis of Biologically Important Angiotensin-II and Angiotensin-IV Peptides by Using 4-(2',4'-Dimethoxypenyl-Fmoc-Aminomethyl)phenoxy Resin

Abstract

In peptide chemistry, there is the goal to produce pure biologically active peptides with the highest possible efficiency, even its possible by chemical synthesis purity and yield as a major problem. In this work, we focus to overcome above difficulty by novel synthetic approach. Angiotensin an oligopeptide is a hormone and a powerful dipsogen, which exhibits a wide range of biological activities, the 8-amino acid sequence Angiotensin-II and 6-amino acid sequence. Angiotensin-IV were synthesized by using 4-(2',4'-dimethoxyphenyl-Fmoc-aminomethyl)phenoxy resin, the modified Fmoc-chemistry and effective hydroxybenzenetriazole, N,N'-diisopropylcarbodiimide coupling and activation methods was used. The yield and chromatographic purities were compared.

Transcriptome analysis of Corvus splendens reveals a repertoire of antimicrobial peptides

“…The mature peptide was synthesized by Fmoc solid-phase synthesis (SPPS) strategy using specific automated peptide synthesizer Autopep-001A 130 . The peptide was amidated at the C-terminus as previous research has shown that amidation at the C-terminal of the peptide is strongly linked to its stability 66 .…”

Synthesis of biologically important neutral amylo-β peptide by using improved Fmoc solid-phase peptide synthetic strategy

“…Estimation of loading (resin capacity measurement) Above synthesized and functionalized resin capacity was measured; the measurement was done by using standard procedures. The calculated resin capacity is 0.71 mmol/g; the resin was characterized by FT-IR spectrometer and SEM analyzer; the resin size and image, functional group of the resin was analyzed [6]. Diisopropylethylamine (DIPEA), 4-dimethylaminopyridine (DMAP), hydroxybenzotriazole (HOBt), diisopropylcarbodiimide (DIC), trifluoroacetic acid (TFA), triisopropylsilane (TIS), pyridine, and piperidine were purchased from Sigma-Aldrich, Germany and China, Alfa Aesar England and Merck Millipore (India).…”

“…Cleavage of peptide from resin After the above synthetic step, the resin was washed with DCM, CHCl 3 , and Methanol and dried [6]. The cleavage was done with 95 %TFA: 2.5 % TIS: 2.5 % water at 2 h under nitrogen atmosphere, and resin was washed two times with TFA; the filtrate was collected and the traces of TFAwas evaporated by using Rota vacuum evaporator.…”

“…Merrifield's technique has undergone a series of modifications and improvements based on the nature of synthetic peptides [5]. The peptide has hydrophobic and hydrophilic nature based on the amino acid present in the target peptide; the hydrophilic nature peptide was somehow easy to synthesis by normal Fmoc chemistry methods, but the hydrophobic and neutral (i.e., 50 % hydrophobic: 50 % hydrophilic) nature peptide was difficult to synthesize due to its salvation and intermolecular aggregation property because total solid-phase peptide synthesis condition is in the homogeneous medium [6]. Even though a lot of synthetic methods are there, mainly the neutral peptide synthesis is a major goal for peptide chemist, so some specific polymer support and synthetic procedure is needed to achieve biologically active neutral peptide synthesis [7].…”

“…Resin containing one -OH group on a tripropylene glycol diacrylate linker attached to 1 % of the polymer was reacted with the -COOH groups of Fmoc amino acids, resulting in strong esterification. Dimethylaminopyridine (DMAP) was used for efficient esterification, followed by reverse amidation coupling of the remaining amino acids with HOBT/DIC in DIEA, which was required for the quantitative reaction on the resin [6]. After coupling of all amino acids, the peptide-resin was treated with TFA in the presence of scavengers to cleave the peptide from the resin.…”