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. Contini
Secondo
;
R. Soave;L. Lo Presti;I. Maffucci;D. Nava;S. Pellegrino;M.L. Gelmi
Penultimo
;
F. Clerici
Ultimo
2015-03-27

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 is
Chemical Engineering (all); Chemistry (all)
Settore CHIM/06 - Chimica Organica
Settore CHIM/02 - Chimica Fisica
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/329952
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