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Article Dans Une Revue Biochimie Année : 1995

The secondary structure of the insect defensin A depends on its environment. A circular dichroism study

M Maget-Dana
  • Fonction : Auteur
J.M Bonmatin
C Hetru
  • Fonction : Auteur
J Maurizot
  • Fonction : Auteur

Résumé

Defensin A is an inducible antibacterial protein isolated from the larvae of Phormia terranovae. The conformation of defensin A has been previously determined by two-dimensional 1H-NMR for concentrations in the range of 4-8 mM in water (Bonmatin JM et al (1992) J Biomol NMR 2, 235-256). CD spectroscopic data of defensin A at lower concentrations (10(-5) to 10(-3) M) are reported herein. The ellipticity in the 200-240 nm wavelength range for various solvents varies as follows: acetonitrile < water < methanol < HFIP. The magnitude of theta 222 is strongly dependent on defensin concentration in a buffer solution, suggesting an aggregation process. The helical content of defensin A is maximum at a pH value range (7.5-8) for which the optimum antibacterial activity was observed (Cociancich S et al (1993) J Biol Chem 268, 19239-19245).
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hal-02082593 , version 1 (13-10-2021)

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M Maget-Dana, J.M Bonmatin, C Hetru, M. Ptak, J Maurizot. The secondary structure of the insect defensin A depends on its environment. A circular dichroism study. Biochimie, 1995, 77 (4), pp.240-4. ⟨10.1016/0300-9084(96)88130-2⟩. ⟨hal-02082593⟩
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