RT Journal Article
T1 Role of the Tryptophan Residues in the Specific interaction of the Sea Anemone Stichodacty la helianthus’s Actinoporin Sticholysin II with Biological Membranes
A1 García Linares, Sara
A1 Maula, Terhi
A1 Rivera de la Torre, Esperanza
A1 Gavilanes, José G.
A1 Slotte, J.Peter
A1 Martínez del Pozo, Álvaro
AB Actinoporins are pore-forming toxins from sea anemones. Upon interaction with sphingomyelin-containing bilayers, they become integral oligomeric membrane structures that form a pore. Sticholysin II from Stichodactyla helianthus contains five tryptophans located at strategic positions; its role has now been studied using different mutants. Results show that W43 and W115 play a eterminant role in maintaining the high thermostability of the protein, while W146 provides specific interactions for protomer−protomer assembly. W110 and W114 sustain the hydrophobic effect, which is one of the major driving forces for membrane binding in the presence of Chol. However, in its absence, additional interactions with sphingomyelin are required. These conclusions were confirmed with two sphingomyelin analogues, one of which had impaired hydrogen bonding properties. The results obtained support actinoporins’ Trp residues playing a major role in membrane recognition and binding, but their residues have an only minor influence on the diffusion and oligomerization steps needed to assemble a functional pore.
PB American Chemical Society
SN 0006-2960
YR 2016
FD 2016
LK https://hdl.handle.net/20.500.14352/23063
UL https://hdl.handle.net/20.500.14352/23063
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
DS Docta Complutense
RD 1 sept 2024