The crystal structure of a Dcp-containing peptide.
We have investigated the conformational preferences of a newly synthesized C(alpha,alpha) symmetrically disubstituted glycine, namely alpha,alpha-dicyclopropylglycine (Dcp). We report here the crystal structure of a fully protected dipeptide containing Dcp, namely Z-Dcp(1)-Dcp(2)-OCH(3). Both Dcp residues are in a folded conformation. The overall peptide structural organization corresponds to an alpha-pleated sheet conformation, similar to that observed in linear peptides made up of alternating D- and L-residues and in Z-Aib-Aib-OCH(3) (Aib: alpha,alpha-dimethylglycine). These preliminary data suggest that the Dcp could represent an alternative as molecular tool to stabilize folded conformations.
De Simone
G
G
Centro Interuniversitario di Ricerca su Peptidi Bioattivi, di Biocristallografia, CNR, University of Napoli "Federico II," via Mezzocannone 4, I-80134 Napoli, Italy.
Lombardi
A
A
Galdiero
S
S
Nastri
F
F
Di Costanzo
L
L
Gohda
S
S
Sano
A
A
Yamada
T
T
Pavone
V
V
D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry*; D005998:Glycine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation
D004151:Dipeptides; C405282:Z-Dcp-Dcp-OCH3; D005998:Glycine