Nα-acylated β2,3-3-azapeptides, or α-hydrazidopeptides, of different lengths were synthesized starting from a conformationally restricted imidazolidinone-tethered monomer. The preferential conformations of the oligomers were investigated by NMR and CD spectroscopy, supported by computational analysis. The experimental data clearly confirmed the tendency of these α-hydrazidopeptides to fold into a zig-zag (Z8) 8-helix conformation, whose stability is length-dependent, stabilized by the C=O(i)···H–N(i + 2) and N(i)···H–N(i + 1) intramolecular H-bonding pattern, as well as by non-standard C=O···H-C hydrogen bonds.

Imidazolidinone-Tethered α-Hydrazidopeptides – Synthesis and Conformational Investigation

Calvaresi M.;
2019

Abstract

Nα-acylated β2,3-3-azapeptides, or α-hydrazidopeptides, of different lengths were synthesized starting from a conformationally restricted imidazolidinone-tethered monomer. The preferential conformations of the oligomers were investigated by NMR and CD spectroscopy, supported by computational analysis. The experimental data clearly confirmed the tendency of these α-hydrazidopeptides to fold into a zig-zag (Z8) 8-helix conformation, whose stability is length-dependent, stabilized by the C=O(i)···H–N(i + 2) and N(i)···H–N(i + 1) intramolecular H-bonding pattern, as well as by non-standard C=O···H-C hydrogen bonds.
2019
Amabili P.; Calvaresi M.; Martelli G.; Orena M.; Rinaldi S.; Sgolastra F.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/717693
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