THE SECONDARY STRUCTURE OF THE INSECT DEFENSIN-A DEPENDS ON ITS ENVIRONMENT - A CIRCULAR-DICHROISM STUDY
Magetdana, R; Bonmatin, JM; Hetru, C; Ptak, M; Maurizot, JC
| HERO ID | 1195021 |
|---|---|
| In Press | No |
| Year | 1995 |
| Title | THE SECONDARY STRUCTURE OF THE INSECT DEFENSIN-A DEPENDS ON ITS ENVIRONMENT - A CIRCULAR-DICHROISM STUDY |
| Authors | Magetdana, R; Bonmatin, JM; Hetru, C; Ptak, M; Maurizot, JC |
| Journal | Biochimie |
| Volume | 77 |
| Issue | 4 |
| Page Numbers | 240-244 |
| Abstract | 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). |
| Doi | 10.1016/0300-9084(96)88130-2 |
| Pmid | 8589051 |
| Is Certified Translation | No |
| Dupe Override | No |
| Comments | Source: Web of Science A1995RC52500003 |
| Is Public | Yes |
| Language Text | English |
| Keyword | DEFENSIN A; INSECT DEFENSIN; ANTIBACTERIAL PROTEIN; SECONDARY STRUCTURE; OLIGOMERIZATION; CIRCULAR DICHROISM |
| Is Qa | No |