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The crystal structure of a Dcp-containing peptide

✍ Scribed by Giuseppina De Simone; Angela Lombardi; Stefania Galdiero; Flavia Nastri; Luigi Di Costanzo; Shin Gohda; Atsuiro Sano; Takashi Yamada; Vincenzo Pavone

Publisher
Wiley (John Wiley & Sons)
Year
2000
Tongue
English
Weight
168 KB
Volume
53
Category
Article
ISSN
0006-3525

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✦ Synopsis

We have investigated the conformational preferences of a newly synthesized C ␣,␣ symmetrically disubstituted glycine, namely ␣,␣-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 ␣-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: ␣,␣-dimethylglycine). These preliminary data suggest that the Dcp could represent an alternative as molecular tool to stabilize folded conformations.

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## Abstract The crystal structure and conformation of the synthetic cyclic tetrapeptide, __cyclo__(L‐Pro‐Sar)~2~, was determined by x‐ray analysis. The peptide crystallizes in the orthorhombic space group __P__2~1~2~1~2~1~ with cell parameters __a__ = 9.277(1), __b__ = 12.884(1), and __c__ = 15.581