caa a22 4500 605512469 CHVBK 20210128100655.0 cr unu---uuuuu 210128e20150401xx s 000 0 eng 10.1007/s00894-015-2622-4 doi (NATIONALLICENCE)springer-10.1007/s00894-015-2622-4 Analysis of the flexibility and stability of the structure of magainin in a bilayer, and in aqueous and nonaqueous solutions using molecular dynamics simulations [Elektronische Daten] [Elham Esmaili, Mohsen Shahlaei] The precise mode of the antimicrobial activity of Magainin (Mag)—an antimicrobial peptide (AMP)—is still unclear. In this study, the conformation of Mag was characterized in water, and in a methanol and lipid bilayer [palmitoyl-oleoylphosphatidylcholine (POPC)] using a molecular dynamics (MD) simulation technique. To describe the role conformation plays in Mag function, the global conformational differences within three systems were studied. Through analysis of the resulting configuration ensembles, the differences in the three systems, such as overall flexibility and average secondary structure, were studied. It is suggested that these differences may be important enough to influence interactions with lipid biomembranes, thereby influencing key properties such as penetration into cell membrane and stability. Graphical Abstract Snapshot of the simulation system for a Magainin (Mag) monomer (peptide is in surfacerepresentation colored by residue). Lipids are shown in gray licorice representation with wateratoms colored green on either side Springer-Verlag Berlin Heidelberg, 2015 Magainin nationallicence Molecular dynamics simulation nationallicence Conformational analysis nationallicence Principal component analysis nationallicence Esmaili Elham Department of Biochemistry, Sanandaj Branch, Islamic Azad University, Sanandaj, Iran aut Shahlaei Mohsen Medical Biology Research Center, Kermanshah University of Medical Sciences, 67346-67149, Kermanshah, Iran aut Journal of Molecular Modeling Springer Berlin Heidelberg 21/4(2015-04-01), 1-15 1610-2940 21:4<1 2015 21 894 https://doi.org/10.1007/s00894-015-2622-4 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00894-015-2622-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Esmaili Elham Department of Biochemistry, Sanandaj Branch, Islamic Azad University, Sanandaj, Iran aut NATIONALLICENCE 700 1- Shahlaei Mohsen Medical Biology Research Center, Kermanshah University of Medical Sciences, 67346-67149, Kermanshah, Iran aut NATIONALLICENCE 773 0- Journal of Molecular Modeling Springer Berlin Heidelberg 21/4(2015-04-01), 1-15 1610-2940 21:4<1 2015 21 894