scholarly journals Convergent Synthesis of Thioether Containing Peptides

Molecules ◽  
2020 ◽  
Vol 25 (1) ◽  
pp. 218
Author(s):  
Spyridon Mourtas ◽  
Christina Katakalou ◽  
Dimitrios Gatos ◽  
Kleomenis Barlos
Keyword(s):  
Carboxylic Acids ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Building Blocks ◽  
Solid Support ◽  
Convergent Synthesis ◽  
Fmoc Group ◽  
Synthetic Routes ◽  
Peptide Elongation

Thioether containing peptides were obtained following three synthetic routes. In route A, halo acids esterified on 2-chlorotrityl(Cltr) resin were reacted with N-fluorenylmethoxycarbonyl (Fmoc) aminothiols. These were either cleaved from the resin to the corresponding (Fmoc-aminothiol)carboxylic acids, which were used as key building blocks in solid phase peptide synthesis (SPPS), or the N-Fmoc group was deprotected and peptide chains were elongated by standard SPPS. The obtained N-Fmoc protected thioether containing peptides were then condensed either in solution, or on solid support, with the appropriate amino components of peptides. In route B, the thioether containing peptides were obtained by the reaction of N-Fmoc aminothiols with bromoacetylated peptides, which were synthesized on Cltr-resin, followed by removal of the N-Fmoc group and subsequent peptide elongation by standard SPPS. In route C, the thioether containing peptides were obtained by the condensation of a haloacylated peptide synthesized on Cltr-resin and a thiol-peptide synthesized either on 4-methoxytrityl(Mmt) or trityl(Trt) resin.

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>

Hydrazine hydrate: A new reagent for Fmoc group removal in solid phase peptide synthesis

2019 ◽  
Vol 60 (1) ◽  
pp. 48-51 ◽  
Author(s):  
Verónica Rodríguez ◽  
Julieth T. Román ◽  
Ricardo Fierro ◽  
Zuly J. Rivera ◽  
Javier E. García
Keyword(s):  
Hydrazine Hydrate ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Fmoc Group

scholarly journals Reinvestigation of a Critical Reductive Amination Step Leads to an Optimized Protocol for the Synthesis of N-2-Hydroxybenzylcysteine Peptide Crypto-Thioesters

2020 ◽  
Author(s):  
Skander Abboud ◽  
Vincent AUCAGNE
Keyword(s):  
Peptide Synthesis ◽  
Reaction Mechanisms ◽  
Reductive Amination ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Building Blocks ◽  
Native Chemical Ligation ◽  
Chemical Ligation ◽  
Optimized Protocol ◽  
Depth Study

An in-depth study of the Fmoc-based solid phase peptide synthesis of N-Hnb-Cys crypto-thioester peptides, advantageous building blocks for the native chemical ligation-based synthesis of proteins, led to the identification of epimerized and imidazolidinone side products formed during a key reductive amination step. The understanding of the underlying reaction mechanisms was crucial for the developement of an automatable optimized synthetic protocol.

scholarly journals Serine promoted synthesis of peptide thioester-precursor on solid support for native chemical ligation

2017 ◽  
Vol 8 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Hader E. Elashal ◽  
Yonnette E. Sim ◽  
Monika Raj
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Solid Support ◽  
Native Chemical Ligation ◽  
Selective Activation ◽  
Chemical Ligation ◽  
Peptide Thioester ◽  
Peptide Thioesters

Fmoc solid phase peptide synthesis of peptide thioesters by displacement of the cyclic urethane moiety obtained by the selective activation of C-terminal serine.

scholarly journals Development of oxetane modified building blocks for peptide synthesis

2020 ◽  
Vol 18 (28) ◽  
pp. 5400-5405 ◽  
Author(s):  
Stefan Roesner ◽  
Jonathan D. Beadle ◽  
Leo K. B. Tam ◽  
Ina Wilkening ◽  
Guy J. Clarkson ◽  
...  
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Building Blocks

The synthesis and use of oxetane modified dipeptide building blocks in solution and solid-phase peptide synthesis (SPPS) is reported.

scholarly journals The 9-Fluorenylmethoxycarbonyl (Fmoc) Group in Chemical Peptide Synthesis – Its Past, Present, and Future

2020 ◽  
Vol 73 (4) ◽  
pp. 271 ◽  
Author(s):  
Wenyi Li ◽  
Neil M. O'Brien-Simpson ◽  
Mohammed Akhter Hossain ◽  
John D. Wade
Keyword(s):  
Chemical Synthesis ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Peptide Bond ◽  
Synthesis Methods ◽  
Protecting Group ◽  
Fmoc Group ◽  
The 1960S ◽  
The Many

The chemical formation of the peptide bond has long fascinated and challenged organic chemists. It requires not only the activation of the carboxyl group of an amino acid but also the protection of the Nα-amino group. The more than a century of continuous development of ever-improved protecting group chemistry has been married to dramatic advances in the chemical synthesis of peptides that, itself, was substantially enhanced by the development of solid-phase peptide synthesis by R. B. Merrifield in the 1960s. While the latter technology has continued to undergo further refinement and improvement in both its chemistry and automation, the development of the base-labile 9-fluorenylmethoxycarbonyl (Fmoc) group and its integration into current synthesis methods is considered a major landmark in the history of the chemical synthesis of peptides. The many beneficial attributes of the Fmoc group, which have yet to be surpassed by any other Nα-protecting group, allow very rapid and highly efficient synthesis of peptides, including ones of significant size and complexity, making it an even more valuable resource for research in the post-genomic world. This review charts the development and use of this Nα-protecting group and its adaptation to address the need for more green chemical peptide synthesis processes.

OctaGel Resin - A New PEG-PS-based Solid Support for Solid-Phase Peptide Synthesis

2019 ◽  
Vol 16 (12) ◽  
pp. 935-940
Author(s):  
Shaveer Ramkisson ◽  
Yahaya E. Jad ◽  
Anamika Sharma ◽  
Beatriz G. de la Torre ◽  
Fernando Albericio
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Solid Support ◽  
Bead Size ◽  
Swelling Capacity ◽  
Surface Active

: OctaGel resin is a unique, highly uniformed surface-active resin. Here, we compared the performance of OctaGel with that of known resins on the market, namely polystyrene and ChemMatrix, in Solid-Phase Peptide Synthesis. The synthesis of the ‘difficult’ Aib-ACP (65-74) decapeptide showed that OctaGel has the potential to yield molecules with satisfactory purity. Given its high swelling capacity and large bead size, OctaGel also shows efficient interaction with various solvents, including those mainly used for SPPS (DMF and DCM).

scholarly journals Solid Phase Peptide Synthesis by Oxidation-Reduction Condensation. Synthesis of LH–RH by Fragment Condensation on Solid Support

1973 ◽  
Vol 46 (10) ◽  
pp. 3240-3247 ◽  
Author(s):  
Rei Matsueda ◽  
Hiroshi Maruyama ◽  
Eiichi Kitazawa ◽  
Hidekuni Takahagi ◽  
Teruaki Mukaiyama
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Solid Support ◽  
Oxidation Reduction ◽  
Fragment Condensation ◽  
Lh Rh

scholarly journals Stirring Peptide Synthesis to a New Level of Efficiency

2021 ◽  
Author(s):  
Johnny N Naoum ◽  
Israel Alshanski ◽  
Guy Mayer ◽  
Poriah Strauss ◽  
Mattan Hurevich
Keyword(s):  
Elevated Temperature ◽  
Peptide Synthesis ◽  
State Of The Art ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Solid Support ◽  
The State ◽  
Large Excess

In this work, a new setup that relies on fast stirring and heating was used to increase the diffusion of both reagents and solid support. we show that the combination of fast mixing and elevated temperature enables the acceleration of solid-phase peptide synthesis without using a large excess of reagents, providing a greener and accessible alternative to the state-of-the-art.<br>

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