[Structure-functional studies of polymyxins. (1)-NMR analysis of polymyxin B and M conformation].
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.
Okhanov
V V
VV
Dubovskiĭ
P V
PV
Miroshnikov
A I
AI
D009682:Magnetic Resonance Spectroscopy; D011112:Polymyxin B / Q000737:chemistry*; D011113:Polymyxins / Q000737:chemistry*; D013329:Structure-Activity Relationship
D011113:Polymyxins; D011112:Polymyxin B
Strukturno-funktsional'nye issledovaniia polimiksinov. (1)IaMR-analiz konformatsii polimiksinov B i M.