Self-assembling properties of all γ-cyclic peptides containing sugar amino acid residues.
In this study, a novel dimer-forming cyclic peptide composed exclusively by cyclic γ-amino acids with a saccharide-like outer surface is described. The antiparallel β-sheet type hydrogen bonding interactions responsible for the large association constant in non-polar solvents constitute a suitable model for a novel class of self-assembling peptide nanotubes.
Departamento de Química Orgánica, Centro Singular de Investigación en Química Biológica y Materiales Moleculares y Unidad Asociada al CSIC, Campus Vida, Universidad de Santiago de Compostela, 15782 Santiago de Compostela, Spain.
Arcadio
A
Guerra
Roberto J
RJ
Brea
Manuel
M
Amorín
Luis
L
Castedo
Juan R
JR
Granja
D000595:Amino Acid Sequence; D000598:Amino Acids, Cyclic / Q000737:chemistry*; D019281:Dimerization; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013400:Sugar Acids / Q000737:chemistry*
D000598:Amino Acids, Cyclic; D010456:Peptides, Cyclic; D013400:Sugar Acids