143327-83-7Relevant articles and documents
Development of a functional cis-prolyl bond biomimetic and mechanistic implications for nickel superoxide dismutase
Tietze, Daniel,Tischler, Marco,Voigt, Stephan,Imhof, Diana,Ohlenschlaeger, Oliver,Goerlach, Matthias,Buntkowsky, Gerd
, p. 7572 - 7578 (2010)
During recent years several peptide-based Ni superoxide dismutase (NiSOD) models have been developed. These NiSOD models show an important structural difference compared to the native NiSOD enzyme, which could cause a completely different mechanism of superoxide dismutation. In the native enzyme the peptide bond between Leu4 and Pro5 is cis-configured, while the NiSOD models exhibit a trans-configured peptide bond between these two residues. To shed light on how the configuration of this single peptide bond influences the activity of the NiSOD model peptides, a new cisprolyl bond surrogate was developed. As surrogate we chose a leucine/alanine-based disubstituted 1,2,3-triazole, which was incorporated into the NiSOD model peptide replacing resi-dues Leu4 and Pro5. The yielded 1,5disubstituted triazole nickel peptide exhibited high SOD activity, which was approximately the same activity as its parent trans-configured analogue. Hence, the conformation of the prolyl peptide bond apparently has of minor importance for the catalytic activity of the metallopeptides as postulated in literature. Furthermore, it is shown that the triazole metallopeptide is forming a stable cyanide adduct as a substrate analogue model complex.
1,5-Disubstituted 1,2,3-Triazole-Containing Peptidotriazolamers: Design Principles for a Class of Versatile Peptidomimetics
Kracker, Oliver,Góra, Jerzy,Krzciuk-Gula, Joanna,Marion, Antoine,Neumann, Beate,Stammler, Hans-Georg,Nie?, Anke,Antes, Iris,Latajka, Rafa?,Sewald, Norbert
supporting information, p. 953 - 961 (2017/12/26)
Peptidotriazolamers are hybrid foldamers combining features of peptides and triazolamers—repetitive peptidomimetic structures with triazoles replacing peptide bonds. We report on the synthesis of a new class of peptidomimetics, containing 1,5-disubstituted 1,2,3-triazoles in an alternating fashion with amide bonds and the analysis of their conformation in solid state and solution. Homo- or heterochiral peptidotriazolamers were obtained from enantiomerically pure propargylamines with stereogenic centers in the propargylic position and α-azido esters by ruthenium-catalyzed azide–alkyne cycloaddition (RuAAC) under microwave conditions in high yields. With such building blocks the peptidotriazolamers are readily available by solution phase synthesis. While the conformation of the homochiral peptidotriazolamer Boc-Ala[5Tz]Phe-Val[5Tz]Ala-Leu[5Tz]Val-OBzl resembles that of a β VIa1 turn, the heterochiral peptidotriazolamer Boc-d-Ala[5Tz]Phe-d-Val[5Tz]Ala-d-Leu[5Tz]Val-OBzl adopts a polyproline-like repetitive structure.
Synthesis of 3′-triazoyl-dinucleotides as precursors of stable Phe-tRNAPhe and Leu-tRNALeu analogues
Santarem, Marco,Fonvielle, Matthieu,Sakkas, Nicolas,Laisné, Guillaume,Chemama, Maryline,Herbeuval, Jean-Philippe,Braud, Emmanuelle,Arthur, Michel,Etheve-Quelquejeu, Mélanie
, p. 3231 - 3233 (2014/07/22)
We report here the synthesis of stable Phe-tRNAPhe and Leu-tRNALeu analogues containing a 1,2,3-triazole ring instead of the ribose-amino acid ester bond. The 1,2,3-triazole ring is generated by dipolar cycloaddition of alkyne Phe and Leu analogues to 3′-azido-3′- deoxyadenosine via the CuI-catalysed Huisgen, Meldal, Sharpless 1,3-cycloaddition. The corresponding triazoyl pdCpA dinucleotides, obtained by classical phosphoramidite chemistry, were enzymatically ligated to 22-nt or 74-nt RNA generating stable Phe-tRNAPhe analogues containing the acceptor stem or full tRNA moieties, respectively. These molecules represent useful tools to study the contribution of the RNA and amino acid moieties in stabilization of aminoacyl-tRNA/protein complexes.
