Abstract
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-hydroxy 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
