66921-96-8Relevant academic research and scientific papers
PENICILLIN-BINDING PROTEIN INHIBITORS
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Paragraph 00273, (2021/06/04)
Described herein are certain boron-containing compounds, compositions, preparations and their use as modulators of the transpeptidase function of bacterial penicillin-binding proteins and as antibacterial agents. In some embodiments, the compounds describ
A NEW MACROCYCLIC DIACID WITH BALANCED CONFORMATIONAL FLEXIBILITY AND PREORGANIZATION
Gennari, Cesare,Molinari, Francesco,Bartoletti, Marcella,Potenza, Donatella
, p. 279 - 282 (2007/10/02)
Macrocyclic diacid 1 was designed and synthesized as an effective catalyst for hemiacetal cleavage.Molecular modelling studies (using Clark Still's MacroModel) show that 1 has many accessible low energy conformations with various degrees of carboxyl group
Acceleration of Hemiacetal Cleavage through Hydrogen Bonding: A New Synthetic Catalyst with Balanced Conformational Flexibility and Preorganization
Gennari, Cesare,Molinari, Francesco,Bartoletti, Marcella,Piarulli, Umberto,Potenza, Donatella
, p. 3201 - 3203 (2007/10/02)
Hemiacetal cleavage catalyst 1 was designed, synthesized, and shown to be effective in promoting glycolaldehyde dimer dissociation and tetramethylglucose mutarotation.
PEPTIDE BOND FORMATION USING AN ENZYME MIMICKING APPROACH
Gennari, Cesare,Molinari, Francesco,Piarulli, Umberto,Bartoletti, Marcella
, p. 7289 - 7300 (2007/10/02)
A man-made enzyme-model based on a concerted proton transfer step (bifunctional catalysis) which mimics the corresponding step in non-ribosomal peptide synthesis was developed.Important features of the model are the following: (a) a bifunctional acid-base catalyst for the thiolester aminolysis rate acceleration, (b) two thiol-containing arms mimicking the "swinging arms" of the enzyme, and (c) symmetry elements so that the process can be iterated with consequent formation of the polypeptide chain.Peptide bond formation was obtained by intramolecularly catalyzed thiolester aminolysis to give 5 in 80percent isolated yield (Scheme IV, V) and with at least a 103-fold rate acceleration in comparison with the corresponding non catalyzed process (4 -> 6)(Scheme IV, Table 1).The reaction is also 4-20 times faster than the analogous process 4 -> 6 run in the presence of 0.1M external catalyst (Et3N-ButCOOH or 2-Pyridone).Important structural and reaction parameters are discussed.A second intramolecular aminolysis reaction gave tripeptide 8 in lower yield (35percent) because of higher steric congestion in the transition state.
