The α-helical second generation peptide dendrimer of sequence (AcAMEA)4(KKLME)2KMKLA is more stable than the corresponding linear peptide AcAMEAAKLMEAMKLA toward pH-induced unfolding and temperature-induced intermolecular aggregation. The effect is interpreted in terms of an α-helix spanning across two successive branching points of the dendrimer. This stabilization effect is unprecedented and opens the way to folded dendritic analogues of proteins using natural amino acids only. Copyright © 2008 American Chemical Society.

Javor, S., Natalello, A., Doglia, S., Reymond, J. (2008). α-helix stabilization within a peptide dendrimer. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 130, 17248-17249 [10.1021/ja8076236].

α-helix stabilization within a peptide dendrimer

NATALELLO, ANTONINO;DOGLIA, SILVIA MARIA;
2008

Abstract

The α-helical second generation peptide dendrimer of sequence (AcAMEA)4(KKLME)2KMKLA is more stable than the corresponding linear peptide AcAMEAAKLMEAMKLA toward pH-induced unfolding and temperature-induced intermolecular aggregation. The effect is interpreted in terms of an α-helix spanning across two successive branching points of the dendrimer. This stabilization effect is unprecedented and opens the way to folded dendritic analogues of proteins using natural amino acids only. Copyright © 2008 American Chemical Society.
Articolo in rivista - Articolo scientifico
dendrimer; secondary structures, conformational stability.
English
17248
17249
Javor, S., Natalello, A., Doglia, S., Reymond, J. (2008). α-helix stabilization within a peptide dendrimer. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 130, 17248-17249 [10.1021/ja8076236].
Javor, S; Natalello, A; Doglia, S; Reymond, J
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/9260
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