A detailed characterization of the behavior of the amphiphilic antimicrobial peptide Trichogin GA IV (TRIC) at the air/water interface during a Langmuir−Blodgett (LB) isotherm is reported. By means of molecular dynamics simulations, experimental data are explained in terms of the conformational changes and aggregate features adopted by TRIC. We show that, due to compression, different structural changes occur: initially formed drop-like aggregates coalesce, forming nanofibers; on increasing the surface tension further, these nanofibers constitute a web-like structure in which meshes are filled by water pools. During these transitions, the peptide chains lie almost parallel to the surface mostly adopting a helical conformation. At high peptide concentration, reaching the maximum of the allowed surface pressure, a monolayer of TRICs in nonhelical conformation and vertically aligned with respect to the air/water interface is formed.
Di Napoli, B., Mazzuca, C., Conflitti, P., Venanzi, M., Palleschi, A. (2018). Behavior of a Peptide during a Langmuir-Blodgett Compression Isotherm: A Molecular Dynamics Simulation Study. JOURNAL OF PHYSICAL CHEMISTRY. C, 122(1), 515-521 [10.1021/acs.jpcc.7b09850].
Behavior of a Peptide during a Langmuir-Blodgett Compression Isotherm: A Molecular Dynamics Simulation Study
Di Napoli, BMembro del Collaboration Group
;Mazzuca, CMembro del Collaboration Group
;Conflitti, PMembro del Collaboration Group
;Venanzi, MMembro del Collaboration Group
;Palleschi, A.
Membro del Collaboration Group
2018-01-01
Abstract
A detailed characterization of the behavior of the amphiphilic antimicrobial peptide Trichogin GA IV (TRIC) at the air/water interface during a Langmuir−Blodgett (LB) isotherm is reported. By means of molecular dynamics simulations, experimental data are explained in terms of the conformational changes and aggregate features adopted by TRIC. We show that, due to compression, different structural changes occur: initially formed drop-like aggregates coalesce, forming nanofibers; on increasing the surface tension further, these nanofibers constitute a web-like structure in which meshes are filled by water pools. During these transitions, the peptide chains lie almost parallel to the surface mostly adopting a helical conformation. At high peptide concentration, reaching the maximum of the allowed surface pressure, a monolayer of TRICs in nonhelical conformation and vertically aligned with respect to the air/water interface is formed.File | Dimensione | Formato | |
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