Supramolecular Interactions of Teixobactin Analogues in the Crystal State.
J Org Chem
; 89(7): 5104-5108, 2024 Apr 05.
Article
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| MEDLINE
| ID: mdl-38506062
ABSTRACT
This Note presents the X-ray crystallographic structure of the N-methylated teixobactin analogue N-Me-d-Gln4,Lys10-teixobactin (1). Eight peptide molecules comprise the asymmetric unit, with each peptide molecule binding a chloride anion through hydrogen bonding with the amide NH group of residues 7, 8, 10, and 11. The peptide molecules form hydrogen-bonded antiparallel ß-sheet dimers in the crystal lattice, with residues 1-3 comprising the dimerization interface. The dimers further assemble end-to-end in the crystal lattice.
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1
Colección:
01-internacional
Banco de datos:
MEDLINE
Idioma:
En
Revista:
J Org Chem
Año:
2024
Tipo del documento:
Article
País de afiliación:
Estados Unidos