Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F18%3A00101183" target="_blank" >RIV/00216224:14740/18:00101183 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bpj.2018.08.012" target="_blank" >http://dx.doi.org/10.1016/j.bpj.2018.08.012</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2018.08.012" target="_blank" >10.1016/j.bpj.2018.08.012</a>

Result language
angličtina
Original language name
Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane
Original language description
Cell-penetrating and some antimicrobial peptides can translocate across lipid bilayers without disrupting the membrane structure. However, the molecular properties required for efficient translocation are not fully understood. We employed the Metropolis Monte Carlo method together with coarse-grained models to systematically investigate free-energy landscapes associated with the translocation of secondary amphiphilic peptides. We studied a-helical peptides with different length, amphiphilicity, and distribution of hydrophobic content and found a common translocation path consisting of adsorption, tilting, and insertion. In the adsorbed state, the peptides are parallel to the membrane plane, whereas, in the inserted state, the peptides are perpendicular to the membrane. Our simulations demonstrate that, for all tested peptides, there is an optimal ratio of hydrophilic/hydrophobic content at which the peptides cross the membrane the easiest. Moreover, we show that the hydrophobicity of peptide termini has an important effect on the translocation barrier. These results provide general guidance to optimize peptides for use as carriers of molecular cargos or as therapeutics themselves.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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