title: Alpha-helix stabilization within a peptide dendrimer.
abstract: The alpha-helical second generation peptide dendrimer of sequence (AcAMEA)(4)(KKLME)(2)KMKLA 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 alpha-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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, CH-3012 Berne, Switzerland.
authors.forename: Sacha
authors.initials: S
authors.lastname: Javor
authors.forename: Antonino
authors.initials: A
authors.lastname: Natalello
authors.forename: Silvia Maria
authors.initials: SM
authors.lastname: Doglia
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Reymond
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002621:Chemistry / Q000379:methods*; D002942:Circular Dichroism / Q000379:methods; D050091:Dendrimers; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
chemical_list: D000596:Amino Acids; D050091:Dendrimers; D010455:Peptides; D011506:Proteins