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 / Amabili P.; Calvaresi M.; Martelli G.; Orena M.; Rinaldi S.; Sgolastra F.. - In: EUROPEAN JOURNAL OF ORGANIC CHEMISTRY. - ISSN 1434-193X. - ELETTRONICO. - 2019:5(2019), pp. 907-917. [10.1002/ejoc.201801427]
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
