scholarly journals β-Nitro-α-amino acids as latent α,β-dehydro-α-amino acid residues in solid-phase peptide synthesis

ARKIVOC ◽  
2004 ◽  
Vol 2004 (10) ◽  
pp. 101-108 ◽  
Author(s):  
Phillip A. Coghlan ◽  
Christopher J. Easton
2015 ◽  
Vol 21 (6) ◽  
pp. 454-460 ◽  
Author(s):  
Keiko Masuda ◽  
Haruka Ooyama ◽  
Kenshiro Shikano ◽  
Kunihiro Kondo ◽  
Megumi Furumitsu ◽  
...  

Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 5035
Author(s):  
Fanny Guzmán ◽  
Adriana Gauna ◽  
Tanya Roman ◽  
Omar Luna ◽  
Claudio Álvarez ◽  
...  

Peptide synthesis is an area with a wide field of application, from biomedicine to nanotechnology, that offers the option of simultaneously synthesizing a large number of sequences for the purpose of preliminary screening, which is a powerful tool. Nevertheless, standard protocols generate large volumes of solvent waste. Here, we present a protocol for the multiple Fmoc solid-phase peptide synthesis in tea bags, where reagent recycling steps are included. Fifty-two peptides with wide amino acid composition and seven to twenty amino acid residues in length were synthesized in less than three weeks. A clustering analysis was performed, grouping the peptides by physicochemical features. Although a relationship between the overall yield and the physicochemical features of the sequences was not established, the process showed good performance despite sequence diversity. The recycling system allowed to reduce N, N-dimethylformamide usage by 25–30% and reduce the deprotection reagent usage by 50%. This protocol has been optimized for the simultaneous synthesis of a large number of peptide sequences. Additionally, a reagent recycling system was included in the procedure, which turns the process into a framework of circular economy, without affecting the quality of the products obtained.


Author(s):  
Javier Eduardo García Castañeda ◽  
Cristian Francisco Vergel Galeano ◽  
Zuly Jenny Rivera Monroy ◽  
Javier Eduardo Rosas Pérez

<p>Solid phase peptide synthesis using the Fmoc/<em>t</em>-Bu strategy (SPPS-Fmoc/tBu) is the most widely used methodology for obtaining synthetic peptides. In this paper, we evaluate the viability of using 4-methylpiperidine as a reagent for deprotection of the amino acid alpha amino group in SPPS-Fmoc/tBu. For this purpose, the peptide (RRWQWRMKKLG) was simultaneously synthesized using 4-methylpiperidine or piperidine for Fmoc removal reagent. The obtained products had similar purities and yields. Finally, 21 peptides were synthesized using 4-methylpiperidine. Our results suggest that is possible to obtain synthetic peptides efficiently by the strategy SPPS-Fmoc/tBu when 4-methylpiperidine was used as reagent to remove Fmoc groups N-alpha protected amino acids.</p>


Author(s):  
luis camacho III ◽  
Bryan J. Lampkin ◽  
Brett VanVeller

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>


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