RT Journal Article
T1 Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin Sticholysin II
A1 Alegre Cebollada, Jorge
A1 Martínez Del Pozo, Álvaro
A1 Gavilanes, José G.
A1 Goormaghtigh, Erik
AB The structure of the actinoporin sticholysin II (StnII) in the pore state was investigated by Fourier transform infraredspectroscopy in the attenuated total reflection configuration. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/cholesterol unilamellarvesicles were employed. The a-helix content increases in;30% upon lipid binding, which agrees with an extension of eightor nine residues at the N-terminal helix. Furthermore, analyses of dichroic spectra show that the extended N-terminal helix wouldhave a 31º tilt with respect to the membrane normal. The orientation of the central beta-sandwich was also estimated. In addition, it wasdetected that StnII alters the orientation of the lipid acyl chains. 1H/2Hexchange experiments sustain a mainly superficial interactionbetween StnII and the membrane, with no protection of the beta-sandwich. The implications of the results in the mechanism of poreformation are discussed.
SN 1542-0086
YR 2007
FD 2007-11
LK https://hdl.handle.net/20.500.14352/52856
UL https://hdl.handle.net/20.500.14352/52856
LA spa
DS Docta Complutense
RD 13 abr 2025