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Insights on the structure-activity relationship of peptides derived from Sticholysin II

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Citation

Lima de Oliveira, A., Maffud Cilli, E., Ros, U., Crusca, E., Lanio, M. E., Alvarez, C., et al. (2018). Insights on the structure-activity relationship of peptides derived from Sticholysin II. Peptide Science, 110(5). doi:10.1002/bip.23097.


Cite as: https://hdl.handle.net/21.11116/0000-000F-C3C6-5
Abstract
Sticholysin II (StII) is a pore-forming actinoporin from the sea anemone Stichodactyla helianthus. A mechanistic model of its action has been proposed: proteins bind to cell membrane, insert their N-termini into the lipid core and assemble into homo-tetramer pores responsible for host-cell death. Because very likely the first 10 residues of StII N-terminus are critical for membrane penetration, to dissect the molecular details of that functionality, we studied two synthetic peptides: StII1-30 and StII16-35 . They show diverse haemolytic and candidacidal activity that correlate with distinct orientations in SDS micelles. NMR shows that StII1-30 partly inserts into the micelle, while StII16-35 lays on the micelle surface. These results justify the diverse concentration dependence of their candidacidal activity supposing a different mechanism of action and providing new hints on StII lytic activity at molecular level. Biotechnological application of these peptides, focused on the development of therapeutic immunocomplexes, may be envisaged.