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, Paolo; Calvaresi, Matteo; Martelli, Gianluca; Orena, Mario; Rinaldi, Samuele; Sgolastra, Federica. - In: EUROPEAN JOURNAL OF ORGANIC CHEMISTRY. - ISSN 1099-0690. - (2018). [10.1002/ejoc.201801427]
Imidazolidinone-Tethered α-Hydrazidopeptides – Synthesis and Conformational Investigation
Paolo Amabili;Gianluca Martelli;Mario Orena;Samuele Rinaldi
;Federica Sgolastra
2018-01-01
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.
