Thionin Antifungal Peptide Synthesis in Transgenic Barley

2012 ◽  
pp. 359-377
Author(s):  
Jianming Fu ◽  
Minesh Patel ◽  
Anna Maria Nuutila ◽  
Ron Skadsen
Keyword(s):  
Peptide Synthesis ◽  
Antifungal Peptide ◽  
Transgenic Barley

A Strategy for Thioamide Incorporation During Fmoc Solid-Phase Peptide Synthesis with Robust Stereochemical Integrity

2019 ◽  
Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller
Keyword(s):  
Amino Acid ◽  
Functional Groups ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Peptide Elongation

We describe a method to protect the sensitive stereochemistry of the thioamide—in analogy to the protection of the functional groups of amino acid side chains—in order to preserve the thioamide moiety during peptide elongation.<br>

Analytical Methods for Solid Phase Peptide Synthesis

2004 ◽  
Vol 8 (4) ◽  
pp. 291-301 ◽  
Author(s):  
Giuseppina Sabatino ◽  
Mario Chelli ◽  
Alberto Brandi ◽  
Anna Papini
Keyword(s):  
Peptide Synthesis ◽  
Analytical Methods ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis

Development and Pharmacokinetics Study of Antifungal Peptide Nanoliposomes by Liquid Chromatography-tandem Mass Spectrometry

2019 ◽  
Vol 15 (4) ◽  
pp. 312-318
Author(s):  
Shuoye Yang
Keyword(s):  
Mass Spectrometry ◽  
Biological Properties ◽  
Pharmacokinetic Property ◽  
Antifungal Peptide ◽  
Simple Liquid ◽  
Physico Chemical ◽  
Liquid Chromatography Tandem Mass ◽  
Pegylated Lipids

Background: The therapeutic ability and application of antifungal peptide (APs) are limited by their physico-chemical and biological properties, the nano-liposomal encapsulation would improve the in vivo circulation and stability. </P><P> Objective: To develop a long-circulating liposomal delivery systems encapsulated APs-CGA-N12 with PEGylated lipids and cholesterol, and investigated through in vivo pharmacokinetics. Methods: The liposomes were prepared and characterized, a rapid and simple liquid chromatographytandem mass spectrometry (LC-MS/MS) assay was developed for the determination of antifungal peptide in vivo, the pharmacokinetic characteristics of APs liposomes were evaluated in rats. Results: Liposomes had a large, unilamellar structure, particle size and Zeta potential ranged from 160 to 185 nm and -0.55 to 1.1 mV, respectively. The results indicated that the plasma concentration of peptides in reference solutions rapidly declined after intravenous administration, whereas the liposomeencapsulated ones showed slower elimination. The AUC(0-∞) was increased by 3.0-fold in liposomes in comparison with standard solution (20 mg·kg-1), the half-life (T1/2) was 1.6- and 1.5-fold higher compared to the reference groups of 20 and 40 mg·kg-1, respectively. Conclusion: Therefore, it could be concluded that liposomal encapsulation effectively improved the bioavailability and pharmacokinetic property of antifungal peptides.

Peptide Synthesis

BIO-PROTOCOL ◽  
2012 ◽  
Vol 2 (14) ◽  
Author(s):  
Zheng Miao ◽  
Zhen Cheng
Keyword(s):  
Peptide Synthesis

Series of sequential polypeptides containing lysine or arginine: Preparation and characterization

1988 ◽  
Vol 53 (1) ◽  
pp. 145-156 ◽  
Author(s):  
Jana Pírková ◽  
Svetlana Churkina ◽  
Vladimír Gut ◽  
Ivo Frič ◽  
Karel Bláha
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Average Molecular Weight ◽  
Basic Amino Acid ◽  
Cd Spectra ◽  
Active Esters ◽  
Marked Tendency

The sequential polypeptides (Lys-Ala)n, (Lys-Ala-Ala)n, (Lys-Ala-Ala-Ala)n, (Lys-Leu-Ala)n, (Lys-Leu-Ala-Ala)n, (Lys-Leu-Ala-Ala-Ala)n, (Lys-Ala-Leu)n, (Lys-Ala-Leu-Ala)n, (Orn-Leu-Ala)n,(Arg-Ala-Ala)n, (Arg-Leu-Ala)n, (Arg-Leu-Ala-Ala)n, (Arg-Ala-Leu)n, and (Arg-Ala-Leu-Ala)n were synthesized by polymerization of active esters (1-succinimidyl or pentafluorophenyl) of the corresponding Nα-deblocked monomers. The monomers were prepared using the usual methods of peptide synthesis in solution. Upon dialysis, the average molecular weight of the polymer was 6 000-9 000 as determined by sedimentation in ultracentrifuge. Polypeptides, containing leucine in addition to the basic amino acid, showed a marked tendency to aggregation. CD spectra of the products were measured for characterization.

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