jo9b02544_si_002.cif (25.51 kB)
Effect on the Conformation of a Terminally Blocked, (E) β,γ-Unsaturated δ‑Amino Acid Residue Induced by Carbon Methylation
dataset
posted on 2019-12-11, 15:08 authored by Giulia Marafon, Alessandro Moretto, David Zanuy, Carlos Alemán, Marco Crisma, Claudio TonioloPeptides are well-known to play a fundamental therapeutic
role
and to represent building blocks for numerous useful biomaterials.
Stabilizing their active 3D-structure by appropriate modifications
remains, however, a challenge. In this study, we have expanded the
available literature information on the conformational propensities
of a promising backbone change of a terminally blocked δ-amino
acid residue, a dipeptide mimic, by replacing its central amide moiety
with an (E) CβCγ alkene unit. Specifically, we have examined by DFT calculations,
X-ray diffraction in the crystalline state, and FT-IR absorption/NMR
spectroscopies in solution the extended vs folded preferences of analogues
of this prototype system either unmodified or possessing single or
multiple methyl group substituents on each of its four −CH2-CHCH-CH2– main-chain carbon atoms.
The theoretical and experimental results obtained clearly point to
the conclusion that increasing the number of adequately positioned
methylations will enhance the preference of the original sequence
to fold, thus opening interesting perspectives in the design of conformationally
constrained peptidomimetics.
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analogueabsorptionδ-main-chainalkeneprototype systemFT-IRmodificationpreferencesolutionacid residueUnsaturatedsequenceTerminallyX-ray diffractionopeningCarbon Methylation Peptidesspectroscopiemethylation3 D-structureconformationallyAminobuilding blocksdipeptideamide moietyConformationterminallyCHbackbone changemethyl group substituentschallengebiomaterialperspectivepeptidomimeticvspropensitieroleResidue InducedconclusionDFT calculationsliterature information
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