| Autor: |
V V, Okhanov, P V, Dubovskiĭ, A I, Miroshnikov |
| Rok vydání: |
1991 |
| Předmět: |
|
| Zdroj: |
Bioorganicheskaia khimiia. 17(12) |
| ISSN: |
0132-3423 |
| Popis: |
Spatial structures of two polymyxin antibiotics are compared by means of one- and two-dimensional 1H NMR spectroscopy. Cyclic parts of polymyxins B and M contain a system of hydrogen bonds including two beta-turns, however, the analysis of coupling constants 3JHN-C alpha H demonstrated that torsional angles phi of peptide bonds of the residues forming beta-turns in polymyxin M depend on the type of the anion. An increase in lability of the polymyxin M cyclic part in comparison with polymyxin B correlated with the selective cleavage of the peptide bond Dab8-Dab9 of this antibiotic with subtilisin. A similar correlation was found for a short analogue of polymyxin B, a cycloheptapeptide. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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