The racemic product of the Betti reaction of 5-chloro-8-hydroxyquinoline, benzaldehyde, and 2-aminopyridine was separated by chiral HPLC to determine which enantiomer inhibited botulinum neurotoxin serotype A. When the enantiomers unexpectedly proved to have comparable activity, the absolute structures of (+)-(R)-1 and (-)-(S)-1 were determined by comparison of calculated and observed circular dichroism spectra. Molecular modeling studies were undertaken in an effort to understand the observed bioactivity and revealed different ensembles of binding modes, with roughly equal binding energies, for the two enantiomers. © 2011 American Chemical Society.
Cardellina, J.H., Vieira, R.C., Eccard, V., Skerry, J., Montgomery, V., Campbell, Y., et al. (2011). Separation of betti reaction product enantiomers: Absolute configuration and inhibition of botulinum neurotoxin A. ACS MEDICINAL CHEMISTRY LETTERS, 2(5), 396-401 [10.1021/ml200028z].
Separation of betti reaction product enantiomers: Absolute configuration and inhibition of botulinum neurotoxin A
Padula D.;Pescitelli G.;
2011-01-01
Abstract
The racemic product of the Betti reaction of 5-chloro-8-hydroxyquinoline, benzaldehyde, and 2-aminopyridine was separated by chiral HPLC to determine which enantiomer inhibited botulinum neurotoxin serotype A. When the enantiomers unexpectedly proved to have comparable activity, the absolute structures of (+)-(R)-1 and (-)-(S)-1 were determined by comparison of calculated and observed circular dichroism spectra. Molecular modeling studies were undertaken in an effort to understand the observed bioactivity and revealed different ensembles of binding modes, with roughly equal binding energies, for the two enantiomers. © 2011 American Chemical Society.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/1111500
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