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| - Is the Peptide Bond Formation Activated by Cu2+ Interactions? Insights from DensityFunctional Calculations
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| - The catalytic role that Cu2+ cations play in the peptide bond formation has been addressed by means ofdensity functional calculations. First, the Cu2+−(glycine)2 → Cu2+−(glycylglycine) + H2O reaction wasinvestigated since mass spectrometry low collision activated dissociation (CAD) spectra of Cu2+−(glycine)2led to the elimination of a water molecule, which suggested that an intracomplex peptide bond formationmight have occurred. Results show that this intracomplex condensation is associated to a very high freeenergy barrier (97 kcal mol-1) and reaction free energy (66 kcal mol-1) because of the loss of metal coordinationduring the reaction. Second, on the basis of the salt-induced peptide formation theory, the condensation reactionbetween two glycines was studied in aqueous solution using discrete water molecules and the conductorpolarized continuum model (CPCM) continuous method. It is found that the synergy between the interactionof glycines with Cu2+ and the presence of water molecules acting as proton-transfer helpers significantlylower the activation barrier (from 55 kcal/mol for the uncatalyzed system to 20 kcal/mol for the Cu2+ solvatedsystem) which largely favors the formation of the peptide bond.
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