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The crystal structure of a Dcp ‐containing peptide
Author(s) -
De Simone Giuseppina,
Lombardi Angela,
Galdiero Stefania,
Nastri Flavia,
Di Costanzo Luigi,
Gohda Shin,
Sano Atsuiro,
Yamada Takashi,
Pavone Vincenzo
Publication year - 2000
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(200002)53:2<182::aid-bip8>3.0.co;2-v
Subject(s) - chemistry , dipeptide , peptide , crystal structure , glycine , stereochemistry , alpha (finance) , crystallography , cyclic peptide , amino acid , biochemistry , construct validity , nursing , patient satisfaction , medicine
We have investigated the conformational preferences of a newly synthesized C α,α symmetrically disubstituted glycine, namely α,α‐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 α‐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: α,α‐dimethylglycine). These preliminary data suggest that the Dcp could represent an alternative as molecular tool to stabilize folded conformations. © 2000 John Wiley & Sons, Inc. Biopoly 53: 182–188, 2000