Self-Organization Ability
of Chiral <i>N</i><sup>α</sup>‑Substituted, <i>N</i><sup>β</sup>‑Boc Protected α‑Hydrazinoacetamides
in the Crystal
and Solution States
Ralph-Olivier Moussodia
Eugénie Romero
Emmanuel Wenger
Brigitte Jamart-Grégoire
Samir Acherar
10.1021/acs.joc.7b01004.s004
https://acs.figshare.com/articles/journal_contribution/Self-Organization_Ability_of_Chiral_i_N_i_sup_sup_Substituted_i_N_i_sup_sup_Boc_Protected_Hydrazinoacetamides_in_the_Crystal_and_Solution_States/5427103
The
limitations of peptides have severely hampered their use in
pharmacology, thus prompting the design of new peptidomimetic foldamers.
This requires precise knowledge of the secondary structure of new
compounds and the ability to predict their folding. Conformational
studies of the basic units of these foldamers can be of invaluable
assistance in designing new bioactive compounds. To this end, we investigated
the conformation of three chiral <i>N</i><sup>α</sup>-substituted, <i>N</i><sup>β</sup>-Boc protected
α-hydrazinoacetamide model compounds containing various side
chains both on the <i>N</i><sup>α</sup>- and <i>C</i><sup>α</sup>-atoms in both the crystal and solution
states. On the basis of IR absorption spectroscopy, NMR, molecular
dynamics calculations and X-ray diffraction experiments, we demonstrated
that these three models adopt conformational preferences, relying
on eight-, six- or five-membered H-bonded pseudocycles (C<sub>8</sub>, C<sub>6</sub> or C<sub>5</sub>), depending on the steric bulk of
both <i>N</i><sup>α</sup>- or <i>C</i><sup>α</sup>-side chains. This study sheds light onto the versatile
folding ability of the specific class of α-<i>N</i><sup>α</sup>-hydrazinopeptides and emphasizes the key role
of the <i>C</i><sup>α</sup>-side chain on the conformational
preference of the folding.
2017-08-29 00:00:00
C α
preference
five-membered H-bonded pseudocycles
ability
Boc
IR absorption spectroscopy
NMR
N α
foldamer
α- N α
chiral N α
side chains
α- hydrazinoacetamide model compounds
X-ray diffraction experiments