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Kaushik, Shilpa; Krishnan, Arthi; Prausnitz, Mark R.; Ludovice, Peter J.

doi:10.1023/a:1011013218494

Cited by 9 publications

(2 citation statements)

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“…On the other hand, changes in the helical structures in the presence of aforementioned nanomicelles can be carefully explored since the peptide helical structure is relatively small. Besides, Magainin2 has extensive antimicrobial activity and also to date is the only antimicrobial peptide that can enhance the transdermal transport of drug molecules. − In the present research, the molecular interactions of six types of polymers and copolymers with maganin2 in three different polymer/copolymer concentrations (100 mg/mL, 200 mg/mL, and 300 mg/mL) were investigated using all-atom MD simulations (Table ).…”

Section: Introductionmentioning

confidence: 99%

Molecular Self-Assembly Strategy for Encapsulation of an Amphipathic α-Helical Antimicrobial Peptide into the Different Polymeric and Copolymeric Nanoparticles

Jafari

Doustdar

Mehrnejad

2018

J. Chem. Inf. Model.

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Encapsulation of peptide and protein-based drugs in polymeric nanoparticles is one of the fundamental fields in controlled-release drug delivery systems. The molecular mechanisms of absorption of peptides to the polymeric nanoparticles are still unknown, and there is no precise molecular data on the encapsulation process of peptide and protein-based drugs. Herein, the self-assembly of different polymers and block copolymers with combinations of the various molecular weight of blocks and the effects of resultant polymer and copolymer nanomicelles on the stability of magainin2, an α-helical antimicrobial peptide, were investigated by means of all-atom molecular dynamics (MD) simulation. The micelle forming, morphology of micellar aggregations and changes in the first hydration shell of the micelles during micelles formation were explored as well. The results showed that the peptide binds to the polymer and copolymer micelles and never detaches during the MD simulation time. In general, all polymers and copolymers simultaneously encapsulated the peptide during micelles formation and had the ability to maintain the helical structure of the peptide, whereas the first hydration shell of the peptide remained unchanged. Among the micelles, the polyethylene glycol (PEG) micelles completely encapsulated magainin2 and, surprisingly, the NMR structure of the peptide was perfectly kept during the encapsulation process. The MD results also indicated that the aromatic and basic residues of the peptide strongly interact with polymers/copolymers and play important roles in the encapsulation mechanism. This research will provide a good opportunity in the design of polymer surfaces for drug delivery applications such as controlled-release peptide delivery systems.

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Section: Introductionmentioning

confidence: 99%

Molecular Self-Assembly Strategy for Encapsulation of an Amphipathic α-Helical Antimicrobial Peptide into the Different Polymeric and Copolymeric Nanoparticles

Jafari

Doustdar

Mehrnejad

2018

J. Chem. Inf. Model.

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“…Our previous work shows that the use of magainin disrupts vesicles that are made from lipid bilayer components representative of those found in human stratum corneum [5], and that magainin administered in a formulation containing an anionic surfactant, N-lauroyl sarcosine (NLS), in 50% ethanol-in-PBS synergistically increased skin permeability. Mechanistic analysis using differential scanning calorimetry, Fourier-transform infrared spectroscopy, and X-ray diffraction suggested that magainin and NLS can increase skin permeability by disrupting stratum corneum lipid structure [6].…”

Section: Introductionmentioning

confidence: 99%

Optimization of transdermal delivery using magainin pore-forming peptide

Kim

Ludovice

Prausnitz

2008

Journal of Physics and Chemistry of Solids

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The skin's outer layer of stratum corneum, which is a thin tissue containing multilamellar lipid bilayers, is the main barrier to drug delivery to the skin. To increase skin permeability, our previous work has shown large enhancement of transdermal permeation using a pore-forming peptide, magainin, which was formulated with N-lauroyl sarcosine (NLS) in 50% ethanol-in-PBS. Mechanistic analysis suggested that magainin and NLS can increase skin permeability by disrupting stratum corneum lipid structure. In this study, our goal was to improve conditions that increase skin permeability by magainin by further optimizing the pretreatment time and concentration of magainin exposure. We found that skin permeability increased with increasing pretreatment time. Skin permeability also increased with increasing magainin concentration up to 1 mM, but was reduced at a magainin concentration of 2 mM. Enhancement of skin permeability to fluorescein (323 Da) up to 35-fold was observed. In contrast, this formulation did not enhance skin permeability to larger molecules, such as calcein (623 Da) and dextran (3,000 Da).

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