Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins

Sticholysin I and II (Sts: St I and St II) are proteins of biomedical interest that form pores upon the insertion of their N-terminus in the plasma membrane. Peptides spanning the N-terminal residues of StI (StI1-31) or StII (StII1-30) can mimic the permeabilizing ability of these toxins, emerging a...

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Veröffentlicht in:	Biochimie 2019-01, Vol.156, p.109-117
Hauptverfasser:	Ros, Uris, Carretero, Gustavo P.B., Paulino, Joana, Crusca, Edson, Pazos, Fabiola, Cilli, Eduardo M., Lanio, Maria E., Schreier, Shirley, Alvarez, Carlos
Format:	Artikel
Sprache:	eng
Schlagworte:	Actinoporin Circular dichroism Cnidarian Venoms - chemistry Hemolytic peptide Membranes, Artificial Organic Chemicals - chemistry Permeabilizing activity Pore-forming toxin Protein Folding Protein Structure, Secondary Sticholysin Structure-Activity Relationship
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