N-terminal peptide (1-92) of Sticholysin II generated by the cleavage with cyanogen bromide interacts with lipid bilayer but does not promote pore formation
Abstract:
Sticholysin II (St II) is a pore-forming toxin produced by the sea anemone Stichodactyla helianthus with a potent hemolytic activity. For an insight into the role of different St II sequence fragments in their interaction with membranes, we carried out protein digestion with cyanogen bromide. This treatment rendered three peptides, one of them (P3) containing the St II N-terminal sequence (amino acids 1 to 92). Neither P2 nor PI (amino acids 102 to 130, and 131 to 157, respectively) exhibit measurable hemolytic activity or interfere with the native St II function. On the other hand, P3 is able to inhibit toxin hemolytic activity. These differences are discussed in terms of their relative capacity to interact with lipidic membranes.
Año de publicación:
2006
Keywords:
- Pore-forming toxin
- Actinoporin
- Sticholysin
- CNBr-derived peptides
Fuente:
Tipo de documento:
Article
Estado:
Acceso restringido
Áreas de conocimiento:
- Bioquímica
- Bioquímica
- Biomateriales
Áreas temáticas:
- Microorganismos, hongos y algas