Facile Synthesis of Peptidyl Salicylaldehyde Esters and Its Use in Cyclic Peptide Synthesis

2013 ◽  
Vol 15 (20) ◽  
pp. 5182-5185 ◽  
Author(s):  
Jun-Feng Zhao ◽  
Xiao-Hong Zhang ◽  
Ying-Jie Ding ◽  
Yong-Sheng Yang ◽  
Xiao-Bao Bi ◽  
...  

2010 ◽  
Vol 12 (14) ◽  
pp. 3254-3257 ◽  
Author(s):  
Kaname Sasaki ◽  
David Crich


2018 ◽  
Vol 14 ◽  
pp. 1112-1119 ◽  
Author(s):  
Dan Liu ◽  
Ya-Li Guo ◽  
Jin Qu ◽  
Chi Zhang

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.





2019 ◽  
Vol 85 (3) ◽  
pp. 1731-1739 ◽  
Author(s):  
Zhenguang Zhao ◽  
Norman Metanis


2019 ◽  
Vol 85 (3) ◽  
pp. 1495-1503 ◽  
Author(s):  
Akihiro Taguchi ◽  
Kiyotaka Kobayashi ◽  
Yan Cui ◽  
Kentaro Takayama ◽  
Atsuhiko Taniguchi ◽  
...  










Biomedicines ◽  
2018 ◽  
Vol 6 (4) ◽  
pp. 99 ◽  
Author(s):  
Klaas Decoene ◽  
Willem Vannecke ◽  
Toby Passioura ◽  
Hiroaki Suga ◽  
Annemieke Madder

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.



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