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000127406 0247_ $$2doi$$a10.1016/j.biochi.2015.06.024
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000127406 037__ $$aDKFZ-2017-03429
000127406 041__ $$aeng
000127406 082__ $$a540
000127406 1001_ $$aRos, Uris$$b0
000127406 245__ $$aDifferences in activity of actinoporins are related with the hydrophobicity of their N-terminus.
000127406 260__ $$aParis [u.a.]$$bElsevier$$c2015
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000127406 520__ $$aActinoporins are pore-forming toxins (PFT) produced by sea anemones with molecular mass around 20 kDa and high affinity for sphingomyelin. The most studied atinoporins are sticholysins I and II (StI/StII) from Stichodactyla helianthus, equinatoxin II (EqtII) from Actinia equina, and fragaceatoxin C (FraC) from Actinia fragacea. Their N-terminal sequences encompassing residues 1-30 seem to be the best candidates for pore formation. This segment comprises an amphipathic α-helix preceded by a more or less hydrophobic segment, depending on the toxin, of around 10 amino acid residues. Although it is clear that the N-terminal is the most variable sequence in this protein family, the role of their hydrophobic segment in not fully understood. Here we show a comparison of StI, StII, EqtII, and FraC activities with that of their respective N-terminal synthetic peptides. The hemolytic and permeabilizing activity of the peptides reproduce qualitatively the behavior of their respective parental proteins and are particularly related to the hydrophobicity of the corresponding 1-10 segment. Furthermore, the dendrogram analysis of actinoporins' N-terminal sequence allows relating differences in alignment with differences in activity among the four toxins. We have also evaluated the penetration depth of the N-terminal segment of StI and StII by using Trp-containing peptide-analogs. Our data suggest that the N-terminus of StII is more deeply buried into the hydrophobic core of the bilayer than that of StI. We hypothesize that the highest activity of StII could be ascribed to a larger hydrophobic continuum, an uninterrupted sequence of non-charged mainly hydrophobic amino acid residues, of its N-terminus promoting a highest ability to partially insert in the membrane core. Moreover, as we show for four related peptides that a higher hydrophobicity contributes to increase the activity, we reinforce the notion that this property must be taken into account to design new potent membranotropic agents.
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000127406 650_7 $$2NLM Chemicals$$aPeptides
000127406 7001_ $$aRodríguez-Vera, Wendy$$b1
000127406 7001_ $$aPedrera, Lohans$$b2
000127406 7001_ $$aValiente, Pedro A$$b3
000127406 7001_ $$aCabezas, Sheila$$b4
000127406 7001_ $$aLanio, María E$$b5
000127406 7001_ $$0P:(DE-HGF)0$$aGarcía-Sáez, Ana J$$b6
000127406 7001_ $$aAlvarez, Carlos$$b7
000127406 773__ $$0PERI:(DE-600)2011725-5$$a10.1016/j.biochi.2015.06.024$$gVol. 116, p. 70 - 78$$p70 - 78$$tBiochimie$$v116$$x0300-9084$$y2015
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000127406 9141_ $$y2015
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