Single Turn Peptide Alpha Helices with Exceptional Stability in Water

Single Turn Peptide Alpha Helices with Exceptional Stability in Water

Cyclic pentapeptides are not known to exist in α-helical conformations. CD and NMR spectra show that specific 20-membered cyclic pentapeptides, Ac−(cyclo-1,5) [KxxxD]-NH2 and Ac-(cyclo-2,6)-R[KxxxD]-NH2, are highly α-helical structures in water and independent of concentration, TFE, denaturants, and...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of the American Chemical Society 2005-03, Vol.127 (9), p.2974-2983
Hauptverfasser: Shepherd, Nicholas E, Hoang, Huy N, Abbenante, Giovanni, Fairlie, David P
Format: Artikel
Sprache:eng
Schlagworte:
Biological and medical sciences
Circular Dichroism
Conformational dynamics in molecular biology
Drug Stability
Fundamental and applied biological sciences. Psychology
Humans
Hydrogen Bonding
Models, Molecular
Molecular biophysics
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides - chemistry
Peptide Hydrolases - chemistry
Peptide Hydrolases - metabolism
Peptides, Cyclic - chemistry
Protein Denaturation
Protein Structure, Secondary
Solvents
Temperature
Water - chemistry
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Cyclic pentapeptides are not known to exist in α-helical conformations. CD and NMR spectra show that specific 20-membered cyclic pentapeptides, Ac−(cyclo-1,5) [KxxxD]-NH2 and Ac-(cyclo-2,6)-R[KxxxD]-NH2, are highly α-helical structures in water and independent of concentration, TFE, denaturants, and proteases. These are the smallest α-helical peptides in water.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0456003