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@article{1438436, author = {Kabelka, Ivo and Vácha, Robert}, article_location = {New York, USA}, article_number = {6}, doi = {http://dx.doi.org/10.1016/j.bpj.2018.08.012}, keywords = {CELL-PENETRATING PEPTIDES; SOLID-STATE NMR; TRANSMEMBRANE HELIX INSERTION; ORIENTED CIRCULAR-DICHROISM; MOLECULAR-DYNAMICS METHOD; ANTIMICROBIAL PEPTIDE; LIPID-BILAYERS; FORCE-FIELD; AMPHIPATHIC PEPTIDES; BUFORIN II}, language = {eng}, issn = {0006-3495}, journal = {Biophysical Journal}, title = {Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane}, volume = {115}, year = {2018} }
TY - JOUR ID - 1438436 AU - Kabelka, Ivo - Vácha, Robert PY - 2018 TI - Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane JF - Biophysical Journal VL - 115 IS - 6 SP - 1045-1054 EP - 1045-1054 PB - Cell Press SN - 00063495 KW - CELL-PENETRATING PEPTIDES KW - SOLID-STATE NMR KW - TRANSMEMBRANE HELIX INSERTION KW - ORIENTED CIRCULAR-DICHROISM KW - MOLECULAR-DYNAMICS METHOD KW - ANTIMICROBIAL PEPTIDE KW - LIPID-BILAYERS KW - FORCE-FIELD KW - AMPHIPATHIC PEPTIDES KW - BUFORIN II N2 - 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. ER -
KABELKA, Ivo and Robert VÁCHA. Optimal Hydrophobicity and Reorientation of Amphiphilic Peptides Translocating through Membrane. \textit{Biophysical Journal}. New York, USA: Cell Press, 2018, vol.~115, No~6, p.~1045-1054. ISSN~0006-3495. Available from: https://dx.doi.org/10.1016/j.bpj.2018.08.012.
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