Ferrocene diamine scaffolds as inductorsof secondary structure in derived peptides

Prethodno opisani ferocenski peptidi I-VII odlikuju se različitim konformacijskim svojstvima. U ovom su radu opisana strukturna svojstva peptida VIIIa (Ac-Ala-NH-Fn-NHBoc, Fn = ferocenilen) pripravljenog iz prekursora VII (Ac-Ala-NH-Fn-COOMe) umetanjem dodatne donorske NH-skupine. Peptidi VIII podvrgnuti su spektroskopskoj analizi (IR, 1H NMR, 2D NOESY) u cilju utvrđivanja njihovog konformacijskog prostora. Pokazalo se da se derivatizacija peptidnih prekursora VII u peptide VIII značajno odrazila na pripadajuća konformacijska svojstva. Dok su konjugati VII bili stabilizirani inter- i intralančanim vodikovim vezama, u njihovim analozima VIII nađene su isključivo interlančane vodikove veze.Previously described ferrocene peptides I-VII exhibit different conformational properties. This study has explored the structural properties of VIIIa (Ac-Ala-NH-Fn-NHBoc, Fn = ferrocenylene) derived from precursors VII (Ac-Ala-NH-Fn-COOMe) by incorporation of additional donor NH-group. In order to examine their conformational properties, peptides VIII were subjectedto spectroscopic analysis (IR, 1H NMR, 2D NOESY). Derivatization of peptide precursors VII into peptides VIII significantly influenced their conformational properties. Since conjugates VII were stabilized through inter- and intrachain hydrogen bonding, interchain hydrogen bonds were exclusively formed in their analogues VIII