Conformational changes in two neurotoxic proteins from snake venoms.
alpha-Neurotoxin from Naja nigricollis and erabutoxin b from Laticauda semifasciata, two homologous neurotoxic proteins, are studied by circular dichroism, ultraviolet spectroscopy and fluorescence in various water/trifluoroethanol mixtures. The data obtained show that the beta structure of alpha-neurotoxin is conserved in water as well as in the organic solvent. By contrast, erabutoxin b changes from the beta-structure in water to the helix type in trifluoroethanol. The latter induces similarly for both toxins a structural modification around tryptophan 29, a residue common to all neurotoxins known to date. The vicinity of tyrosine 25, another common amino acid, is also altered by the presence of the organic solvent as demonstrated by the sudden increase of reactivity of the phenolic ring towards iodine. The present work affords some evidence for the presence of a particular structure located around the two aromatic residues, which is common to all neurotoxins and able to rearrange independently from the rest of the molecule. Biological importance of this peculiar region is highly probable.
D000818:Animals; D002942:Circular Dichroism; D004220:Disulfides / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D012910:Snake Venoms; D013056:Spectrophotometry, Ultraviolet; D014118:Toxins, Biological; D014443:Tyrosine / Q000032:analysis
D004220:Disulfides; D012910:Snake Venoms; D014118:Toxins, Biological; D014443:Tyrosine