2019
DOI: 10.1016/j.biochi.2018.10.005
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Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins

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Cited by 7 publications
(9 citation statements)
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“…We have previously proposed that the higher permeabilizing activity of StII1-30 could be ascribed to its higher propensity to fold and pre-associate as coiled-coil structures in solution, without the assistance of the membrane (29). The results of this work support the hypothesis that pre-association in solution is an essential prerequisite for the poreforming activity of StII1-30.…”
Section: Discussionsupporting
confidence: 82%
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“…We have previously proposed that the higher permeabilizing activity of StII1-30 could be ascribed to its higher propensity to fold and pre-associate as coiled-coil structures in solution, without the assistance of the membrane (29). The results of this work support the hypothesis that pre-association in solution is an essential prerequisite for the poreforming activity of StII1-30.…”
Section: Discussionsupporting
confidence: 82%
“…Previous structural studies based on low-resolution circular dichroism measurements of StII1-30 have shown that this peptide is able to adopt α-helical secondary structure and self-associate forming coiled-coil structures in solution without the assistance of the membrane (9,29). Therefore, we performed atomistic MD simulations to get preassociated StII1-30 in solution.…”
Section: Iii1 Pre-associated In Solution Stii1-30 Forms Pores In Lipmentioning
confidence: 99%
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“…According to the Eisenberg plot [55], NAPHT-BP100 overall hydrophobicity (<H> = 0.409) and significant hydrophobic moment (<µH> = 0.737) classify the peptide-formed helix as "membrane surface seeking". In addition, it has been reported that slight variations in peptide sequence, thus in its hydrophobicity and hydrophobic moment, can trigger considerable changes in the peptide-membrane interaction and permeabilizing capabilities of the peptide [56,57]. Changes in liposome size and size distribution, and zeta potential triggered by NAPHT-BP100 were measured using dynamic light scattering (Figure 7), revealing that membrane charge neutralization plays an important role in membrane destabilization, ultimately causing lipid aggregation.…”
Section: Discussionmentioning
confidence: 97%