scholarly journals Recyclable hypervalent-iodine-mediated solid-phase peptide synthesis and cyclic peptide synthesis

2018 ◽  
Vol 14 ◽  
pp. 1112-1119 ◽  
Author(s):  
Dan Liu ◽  
Ya-Li Guo ◽  
Jin Qu ◽  
Chi Zhang
Keyword(s):  
Peptide Synthesis ◽  
Cyclic Peptide ◽  
Solid Phase ◽  
Biological Activities ◽  
Solid Phase Peptide Synthesis ◽  
Coupling Reaction ◽  
Hypervalent Iodine ◽  
Peptide Coupling ◽  
Cyclic Peptide Synthesis ◽  
Cyclic Heptapeptide

The system of the hypervalent iodine(III) reagent FPID and (4-MeOC6H4)3P was successfully applied to solid-phase peptide synthesis and cyclic peptide synthesis. Four peptides with biological activities were synthesized through SPPS and the bioactive cyclic heptapeptide pseudostellarin D was obtained via solution-phase peptide synthesis. It is worth noting that FPID can be readily regenerated after the peptide coupling reaction.

scholarly journals Pyrrole-Mediated Peptide Cyclization Identified through Genetically Reprogrammed Peptide Synthesis

Biomedicines ◽  
2018 ◽  
Vol 6 (4) ◽  
pp. 99 ◽  
Author(s):  
Klaas Decoene ◽  
Willem Vannecke ◽  
Toby Passioura ◽  
Hiroaki Suga ◽  
Annemieke Madder
Keyword(s):  
Peptide Synthesis ◽  
Cyclic Peptide ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Screening Method ◽  
In Vitro Translation ◽  
Side Chain ◽  
One Pot ◽  
Depth Analysis

Flexible in vitro translation (FIT) was used as a screening method to uncover a new methodology for peptide constraining based on the attack of a nucleophilic side-chain functionality onto an oxidized furylalanine side chain. A set of template peptides, each containing furylalanine as furan-modified amino acid and a nucleophilic residue (Cys, His, Lys, Arg, Ser, or Tyr), was produced through FIT. The translation mixtures were treated with N-bromosuccinimide (NBS) to achieve selective furan oxidation and subsequent MALDI analysis demonstrated Lys and Ser as promising residues for cyclisation. Solid-phase peptide synthesis (SPPS) was used to synthesize suitable amounts of material for further in-depth analysis and characterisation. It was found that in the case of the peptide containing lysine next to a furylalanine residue, a one-pot oxidation and reduction reaction leads to the generation of a cyclic peptide featuring a pyrrole moiety as cyclisation motif, resulting from the attack of the lysine side chain onto the oxidized furylalanine side chain. Structural evidence was provided via NMR and the generality of the methodology was explored. We hereby expand the scope of our previously developed furan-based peptide labeling and crosslinking strategy.

scholarly journals Novel Cyclic Lipopeptide Antibiotics: Effects of Acyl Chain Length and Position

2020 ◽  
Vol 21 (16) ◽  
pp. 5829 ◽  
Author(s):  
Signe Kaustrup Jensen ◽  
Thomas T. Thomsen ◽  
Alberto Oddo ◽  
Henrik Franzyk ◽  
Anders Løbner-Olesen ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Fatty Acid ◽  
Chain Length ◽  
Peptide Synthesis ◽  
Hemolytic Activity ◽  
Cyclic Peptide ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Resistant Bacteria ◽  
Cyclic Lipopeptide

Multidrug-resistant bacteria are a global health problem. One of the last-resort antibiotics against Gram-negative bacteria is the cyclic lipopeptide colistin, displaying a flexible linker with a fatty acid moiety. The aim of the present project was to investigate the effect on antimicrobial activity of introducing fatty acid moieties of different lengths and in different positions in a cyclic peptide, S3(B), containing a flexible linker. The lipidated analogues of S3(B) were synthesized by 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase peptide synthesis. Following assembly of the linear peptide by Fmoc solid-phase peptide synthesis, on-resin head-to-tail cyclization and fatty acid acylation were performed. The antimicrobial activity was determined against the ESKAPE pathogens, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Escherichia coli. Furthermore, hemolytic activity was determined against human erythrocytes. A total of 18 cyclic lipopeptides were synthesized and characterized. It was found that introduction of fatty acids in positions next to the flexible linker was more strongly linked to antimicrobial activity. The fatty acid length altered the overall hydrophobicity, which was the driving force for both high antimicrobial and hemolytic activity. Peptides became highly hemolytic when carbon-chain length exceeded 10 (i.e., C10), overlapping with the optimum for antimicrobial activity (i.e., C8–C12). The most promising candidate (C8)5 showed antimicrobial activity corresponding to that of S3(B), but with an improved hemolytic profile. Finally, (C8)5 was further investigated in a time-kill experiment.

scholarly journals Sintesis Tiga Peptida Bergugus Pelindung sebagai Prekursor Komponen Vaksin Influenza Universal

2015 ◽  
Vol 15 (2) ◽  
pp. 84 ◽  
Author(s):  
Toto Subroto ◽  
Ari Hardianto ◽  
Abdul Alim Kahari ◽  
Tika Pradnjaparamita
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Coupling Reaction ◽  
Synthesis Strategy ◽  
Helper Epitope ◽  
Universal Influenza Vaccine ◽  
Layer Chromatography ◽  
Conventional Vaccine

Current highly effective conventional vaccine to halt the spread of bird flu has not been invented yet because of susceptiblemutation of influenza virus. In spite of undergoing mutation which causes the amino acid sequence change, influenzaviruses maintain conservation at ectodomain of M2 protein, especially M2e(2-16) (SLLTEVETPIRNEW). The use ofconserved epitope M2e(2-16) in epitope-based vaccine potentially produces universal influenza vaccine. In designingepitope-based vaccine, the M2e(2-16) needs to be coupled with T helper epitope, P25, which is subsequently mentioned asM2e(2-16)-K-P25 (SLLTEVETPIRNEWGKKKL IPNASLIENCTKAEL). The M2e(2-16)-K-P25 was synthesized usingconvergent solid phase peptide synthesis strategy because of the size of the sequence. In this strategy, four peptideprecursors of M2e(2-16)-K-P25; SLLTEVETP (F1), IRNEWGK (F2), KLIPNASLI (F3), and ENCTKAEL (F4); were synthesizedin advance. After the precursors ready, coupling reaction was performed to obtain M2e(2-16)-K-P25. In the previousresearch, F3 has been obtained in high purity through Fmoc/tBu solid phase peptide synthesis method. In this conductedresearch, the three remaining precursors; F1, F2, and F4; were synthesized by the same method. Each peptide was analysedby thin layer chromatography, HPLC, and mass spectroscopy methods. F1, F2 and F4 were successfully synthesized andeach of them was detected at 1490.0, 1874.8 and 1881.9 amu, respectively. However, F1 was not possible to purify becauseof its insolubility in various solvents.

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
Sign in / Sign up

Export Citation Format

Share Document