The properties of the constrained tetrasubstituted 3-sulfanylnorbornene amino acid (NRB), when inserted in Ala-Aib model peptides, were extensively studied. The conformational behaviour of these models was evaluated by theoretical calculations, spectroscopic analyses and by X-ray crystallography. Taken together, our data confirm that both (R,R,R,S)- and (S,S,S,R)-NRB enantiomers possess a strong helicogenic effect when inserted in short Ala-Aib sequences, suggesting that the rigid norbornane core has a positive effect on the ability to stabilize helical secondary structures. This information will be essential for future applications in the rational design of conformationally stable peptides targeted on protein-protein interaction (PPI) surfaces. This journal is
Model peptides containing the 3-sulfanylnorbornene amino acid, a conformationally constrained cysteine analogue effective inducer of 3(10)-helix secondary structures / A. Ruffoni, A. Contini, R. Soave, L. Lo Presti, I. Esposto, I. Maffucci, D. Nava, S. Pellegrino, M.L. Gelmi, F. Clerici. - In: RSC ADVANCES. - ISSN 2046-2069. - 5:41(2015 Mar 27), pp. 32643-32656. [10.1039/c5ra03805g]
Model peptides containing the 3-sulfanylnorbornene amino acid, a conformationally constrained cysteine analogue effective inducer of 3(10)-helix secondary structures
A. Ruffoni
Primo
;A. ContiniSecondo
;R. Soave;L. Lo Presti;I. Maffucci;D. Nava;S. Pellegrino;M.L. GelmiPenultimo
;F. ClericiUltimo
2015
Abstract
The properties of the constrained tetrasubstituted 3-sulfanylnorbornene amino acid (NRB), when inserted in Ala-Aib model peptides, were extensively studied. The conformational behaviour of these models was evaluated by theoretical calculations, spectroscopic analyses and by X-ray crystallography. Taken together, our data confirm that both (R,R,R,S)- and (S,S,S,R)-NRB enantiomers possess a strong helicogenic effect when inserted in short Ala-Aib sequences, suggesting that the rigid norbornane core has a positive effect on the ability to stabilize helical secondary structures. This information will be essential for future applications in the rational design of conformationally stable peptides targeted on protein-protein interaction (PPI) surfaces. This journal isFile | Dimensione | Formato | |
---|---|---|---|
Ruffoni_Contini_Soave_Lo-Presti_Esposto_Maffucci_Nava_Pellegrino_Gelmi_Clerici_RSC_Adv_2015_41_32643-32656.pdf
accesso aperto
Tipologia:
Publisher's version/PDF
Dimensione
1.07 MB
Formato
Adobe PDF
|
1.07 MB | Adobe PDF | Visualizza/Apri |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.