Minimal Helix in the Ferrocene Peptide (CROSBI ID 649883)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa
Podaci o odgovornosti
Nuskol, Marko ; Kodrin, Ivan ; Đaković, Marijana ; Šupljika, Filip ; Čakić Semenčić, Mojca
engleski
Minimal Helix in the Ferrocene Peptide
We have recently demonstrated that introduction of minimal peptide sequence on aminoferrocene may induce the formation of a β-turn-like structures in solution as well as in the solid state of the derived Boc-(AA)2-NH-Fc peptides. As a continuation of the previous work, we have synthesized higher analogues of these bioconjugates with a potential to form minimum sized peptide helices. Herein, we present the extensive study of conformational preferences of Boc-D-Pro-L-Pro-L-Ala-NH-Fc using NMR-, IR- and CD-spectroscopy, X-ray diffraction and DFT calculations. Results obtained from various techniques indicate that dominant conformation of I is stabilized by two intramolecular hydrogen bonds and ordered in a helical manner in solution as well as in the solid state.
Ferrocene ; Peptide ; Conformational Analysis
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Podaci o prilogu
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2017.
objavljeno
Podaci o matičnoj publikaciji
Juribašić Kulcsár, Marina ; Halasz, Ivan
Zagreb:
978-953-7941-15-4
Podaci o skupu
Solid-State Science & Research
poster
01.01.2017-01.01.2017
Zagreb, Hrvatska