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The secondary structure of the insect defensin A depends on its environment. A circular dichroism study.
Maget-Dana, R; Bonmatin, J M; Hetru, C; Ptak, M; Maurizot, J C.
Afiliación
  • Maget-Dana R; Centre de Biophysique Moléculaire (CNRS), Université d'Orléans, France.
Biochimie ; 77(4): 240-4, 1995.
Article en En | MEDLINE | ID: mdl-8589051
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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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Defensinas / Hormonas de Insectos Límite: Animals Idioma: En Revista: Biochimie Año: 1995 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Francia
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Defensinas / Hormonas de Insectos Límite: Animals Idioma: En Revista: Biochimie Año: 1995 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Francia