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Insights on the structure‐activity relationship of peptides derived from Sticholysin II
Author(s) -
Lima de Oliveira Aline,
Maffud Cilli Eduardo,
Ros Uris,
Crusca Jr Edson,
Lanio María Eliana,
Alvarez Carlos,
Schreier Shirley,
Aguiar Pertinhez Thelma,
Spisni Alberto
Publication year - 2018
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/bip.23097
Subject(s) - micelle , critical micelle concentration , tetramer , biophysics , biology , biochemistry , peptide , mechanism of action , microbiology and biotechnology , chemistry , enzyme , aqueous solution , in vitro
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: 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.