Behavior of a Peptide During a Langmuir–Blodgett Compression Isotherm: A Molecular Dynamics Simulation Study

Napoli, Benedetta Di; Meisina, Claudia; Conflitti, Paolo; Venanzi, Mariano; Palleschi, Antonio

doi:10.1021/acs.jpcc.7b09850

Cited by 7 publications

(15 citation statements)

References 47 publications

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“…As for the self‐assembly process leading to small aggregates nucleating the growth of micrometric structures, very recently we carried out MD simulation studies on the aggregation of TrGA at the air/water interface varying the peptide concentration on the aqueous surface . We found that for a number of peptide molecules comprised between n =2 and 8 (corresponding to a Mma per peptide between 2500 and 950 Å 2 /molecule) TrGA forms small drops based on its mixed helical conformation arranged parallel to the surface.…”

Section: Resultsmentioning

confidence: 99%

“…A cut‐off of 1.4 nm for the electrostatic (PME algorithm) and the van der Waals interactions was selected, and temperature and pressure with semi‐isotropic conditions were controlled by the Berendsen algorithm . Topologies for all of the amino acids have been already reported . All simulation analyses were performed during the last 10 ns of simulation time.…”

Section: Methodsmentioning

confidence: 99%

“…[43] Topologies for all of the amino acids have been already reported. [20] All simulation analyses were performed during the last 10 ns of simulation time. The secondary structures were analysed using the DSSP (Define Secondary Structures of Proteins) GROMACS tool and visualized with the VMD software.…”

Section: Molecular Dynamics Simulationsmentioning

confidence: 99%

“…LB peptide films showed a rich morphology, like ′butterfly shapes′, rectangles, dots, nanofibers or nanoribbons. Very recently, some of us characterized by molecular dynamics (MD) simulations the behaviour of TrGA at the air/water interface during a LB compression . It was shown that, on increasing the surface pressure, several structural changes take place: at first, globular aggregates coalesce giving rise to fibrillization.…”

Section: Introductionmentioning

confidence: 99%

“…Very recently, some of us characterized by molecular dynamics (MD) simulations the behaviour of TrGA at the air/water interface during a LB compression. [20] It was shown that, on increasing the surface pressure, several structural changes take place: at first, globular aggregates coalesce giving rise to fibrillization. Then, nanofibers form a network in which meshes are filled by water pools.…”

Section: Introductionmentioning

confidence: 99%

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Controlling the Formation of Peptide Films: Fully Developed Helical Peptides are Required to Obtain a Homogenous Coating over a Large Area

et al. 2019

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The influence of conformational dynamics on the self‐assembly process of a conformationally constrained analogue of the natural antimicrobial peptide Trichogin GA IV was analysed by spectroscopic methods, microscopy imaging at nanometre resolution, and molecular dynamics simulations. The formation of peptide films at the air/water interface and their deposition on a graphite or a mica substrate were investigated. A combination of experimental evidence with molecular dynamics simulation was used to demonstrate that only the fully developed helical structure of the analogue promotes formation of ordered aggregates that nucleate the growth of micrometric rods, which give rise to homogenous coating over wide regions of the hydrophilic mica. This work proves the influence of helix flexibility on peptide self‐organization and orientation on surfaces, key steps in the design of bioinspired organic/inorganic hybrid materials.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Molecular Dynamics Simulationsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Controlling the Formation of Peptide Films: Fully Developed Helical Peptides are Required to Obtain a Homogenous Coating over a Large Area

et al. 2019

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Life at the interface: Engineering bio‐nanomaterials through interfacial molecular self‐assembly

Miller,

Medina

2024

WIREs Nanomed Nanobiotechnol

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Interfacial self‐assembly describes the directed organization of molecules and colloids at phase boundaries. Believed to be fundamental to the inception of primordial life, interfacial assembly is exploited by a myriad of eukaryotic and prokaryotic organisms to execute physiologic activities and maintain homeostasis. Inspired by these natural systems, chemists, engineers, and materials scientists have sought to harness the thermodynamic equilibria at phase boundaries to create multi‐dimensional, highly ordered, and functional nanomaterials. Recent advances in our understanding of the biophysical principles guiding molecular assembly at gas–solid, gas–liquid, solid–liquid, and liquid–liquid interphases have enhanced the rational design of functional bio‐nanomaterials, particularly in the fields of biosensing, bioimaging and biotherapy. Continued development of non‐canonical building blocks, paired with deeper mechanistic insights into interphase self‐assembly, holds promise to yield next generation interfacial bio‐nanomaterials with unique, and perhaps yet unrealized, properties.This article is categorized under: Nanotechnology Approaches to Biology > Nanoscale Systems in Biology Therapeutic Approaches and Drug Discovery > Emerging Technologies

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Molecular Sponge: pH-Driven Reversible Squeezing of Stimuli-Sensitive Peptide Monolayers

et al. 2019

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The cyclic change of structure, thickness, and density, with pH switching from acidic (pH = 3) to basic (pH = 11) condition, has been revealed for chemisorbed monolayers of the peptide Lipo-Aib-Lys-Leu-Aib-Lys-Lys-Leu-Aib-Lys-Ile-Lol, a trichogin GA IV-analogue carrying Lys residues instead of Gly ones at positions 2, 5, 6, and 9, while a homologous peptide not containing Lys residues does not show any response to pH changes. Experimental and theoretical results, obtained by means of quartz crystal microbalance with dissipation monitoring, surface plasmon resonance, nanoplasmonic sensing technique, Fourier transform infrared-reflection attenuated spectroscopy and dynamic force spectroscopy, and molecular dynamics simulations provide detailed information on the overall monolayer structure changes with pH, including the analysis of the intra- and interchain peptide dynamics, the structure of the peptide layer/water/solid interface, as well as the position and role of solvation and nonsolvation water. The observed stimuli-responsive behavior of L1 peptide monolayers is accounted in terms of the occurrence of a pH-induced wetting/dewetting process, due to the pH-induced switching of the hydrophilic character of charged lysine groups to hydrophobic one of the same uncharged groups, along the peptide chain. This behavior in turn promotes the collective change of the aggregation state of the peptide chains. The present results may pave the way to critically reexamine the mechanism of stimuli-responsive systems.

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Behavior of a Peptide During a Langmuir–Blodgett Compression Isotherm: A Molecular Dynamics Simulation Study

Cited by 7 publications

References 47 publications

Controlling the Formation of Peptide Films: Fully Developed Helical Peptides are Required to Obtain a Homogenous Coating over a Large Area

Controlling the Formation of Peptide Films: Fully Developed Helical Peptides are Required to Obtain a Homogenous Coating over a Large Area

Life at the interface: Engineering bio‐nanomaterials through interfacial molecular self‐assembly

Molecular Sponge: pH-Driven Reversible Squeezing of Stimuli-Sensitive Peptide Monolayers

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