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Peptides from RuAAC- Derived 1,5-Disubstituted Triazole Units

Johan R. Johansson (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Elin Hermansson (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Bengt Nordén (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; Nina Kann (Institutionen för kemi- och bioteknik, Organisk kemi) ; Tamas Beke-Somfai (Institutionen för kemi- och bioteknik, Fysikalisk kemi)
European Journal of Organic Chemistry (1434-193X). Vol. 2014 (2014), 13, p. 2703-2713.
[Artikel, refereegranskad vetenskaplig]

Non-natural peptides with structures and functions similar to natural peptides have emerged lately in biomedical as well as nanotechnological contexts. They are interesting for pharmaceutical applications since they can adopt structures with new targeting potentials and because they are generally not prone to degradation by proteases. We report here a new set of peptidomimetics derived from -peptides, consisting of n units of a 1,5-disubstituted 1,2,3-triazole amino acid (5Tzl). The monomer was prepared using ruthenium-catalyzed azide-alkyne cycloaddition (RuAAC) chemistry using [RuCl2Cp*](x) as the catalyst, allowing for simpler purification and resulting in excellent yields. This achiral monomer was used to prepare peptide oligomers that are water soluble independent of peptide chain length. Conformational analysis and structural investigations of the oligomers were performed by 2D NOESY NMR experiments, and by quantum chemical calculations using the B97X-D functional. These data indicate that several conformations may co-exist with slight energetic differences. Together with their increased hydrophilicity, this feature of homo-5Tzl may prove essential for mimicking natural peptides composed of -amino acids, where the various secondary structures are achieved by side chain effects and not by the rigidity of the peptide backbone. The improved synthetic method allows for facile variation of the 5Tzl amino acid side chains, further increasing the versatility of these compounds.

Nyckelord: Foldamers; Conformation analysis; Peptidomimetics; Nitrogen heterocycles; Cycloaddition; Click chemistry

Denna post skapades 2014-07-02. Senast ändrad 2016-01-08.
CPL Pubid: 200077


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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)
Institutionen för kemi- och bioteknik, Organisk kemi (2006-2014)


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