Online article for Non-subscribers

Pay per view

Heterocycles has a pay-per-view service for Non-subscribers.
You will be able to directly purchase the full text article through PayPal.
Your purchased Paper can be downloaded after the payment is completed.
An e-mail will be sent the URL to download the paper.
If you have any questions, please contact:

Price: ¥ 4,320 (Yen only)
Period: This Article can be accessed for 7 days.

Paper | Special issue | Vol 82, No. 1, 2010, pp.729-737
Published online, 22nd July, 2010
DOI: 10.3987/COM-10-S(E)52
Crystal-State Structure Analysis of β-Hydroxy-γ-lactam Constrained Ser/Thr Peptidomimetics

Daniel J. St-Cyr, Thierry Maris, and William D. Lubell*

*Department of Chemistry, University of Montreal, CP 6128, Succursale-Centre-Ville
Montreal, Quebec, H3C 3J7, Canada


Crystallographic evidence has been obtained in support of the ability of β-hydroxy-α-amino-γ-lactams to induce β-turn conformations within peptides. Two dipeptide model systems of these β-hydroxylated variants of the so-called Freidinger-Veber lactams were prepared from the reaction of N-(Fmoc)oxiranylglycine 2 with methyl m-amino benzoate and methyl lysinate, respectively, and crystallized from benzene or ether. In the solid-state, the lactam moiety was found to adopt dihedral angle geometry similar to extended as well as type II β-turn conformations contingent on the C-terminal amino ester moiety. The β-hydroxyl group of the trans-isomer was shown to point away from the turn suggesting its potential for interaction with receptors in conformationally rigid mimics of serine and threonine-containing peptides.