Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously.
This article describes a strategy to develop, starting from a de novo design, bivalent peptides containing two different (alpha-helix and beta-hairpin) and independent secondary-structure elements. The design was based on the use of conformationally restricted peptide libraries. Structural characterization by NMR revealed that the peptides were stable and did not show any long-range NOE interactions between the N-terminal beta-hairpin and the C-terminal alpha-helix. These results suggest that the two elements of secondary structure are stable and well folded.
Pantoja-Uceda
David
D
Department of Medicinal Chemistry, Centro de Investigación Príncipe Felipe, Avda Autopista del Saler, 16. Valencia, Spain.
Pastor
M Teresa
MT
Salgado
Jesús
J
Pineda-Lucena
Antonio
A
Pérez-Payá
Enrique
E
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
D010455:Peptides