Insights on the structure-activity relationship of peptides derived from Sticholysin II
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Wiley-Blackwell
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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: StII(1-30) and StII(16-35). They show diverse haemolytic and candidacidal activity that correlate with distinct orientations in SDS micelles. NMR shows that StII(1-30) partly inserts into the micelle, while StII(16-35) 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.
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candidacidal activity, hemolytic activity, NMR, pore formation, structure-activity relationship
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Inglês
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Peptide Science. Hoboken: Wiley, v. 110, n. 5, 9 p., 2018.
