Peptide nanovesicles formed by the self-assembly of branched amphiphilic peptides
| العنوان: | Peptide nanovesicles formed by the self-assembly of branched amphiphilic peptides |
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| المؤلفون: | Jian Gao, Jianhan Chen, Yasuaki Hiromasa, Takeo Iwamoto, John M. Tomich, L. Adriana Avila, Sushanth Gudlur, Pinakin Sukthankar |
| المصدر: | PLoS ONE, Vol 7, Iss 9, p e45374 (2012) PLoS ONE |
| بيانات النشر: | Public Library of Science (PLoS), 2012. |
| سنة النشر: | 2012 |
| مصطلحات موضوعية: | Proteomics, Drugs and Devices, Drug Research and Development, Materials Science, Lipid Bilayers, lcsh:Medicine, Peptide, 02 engineering and technology, Glycerophospholipids, 010402 general chemistry, 01 natural sciences, Biochemistry, Material by Attribute, Hydrophobic effect, chemistry.chemical_compound, Drug Discovery, Peptide synthesis, Molecular self-assembly, Synthetic Peptide, Nanotechnology, Animals, Lipid bilayer, lcsh:Science, Biology, Cells, Cultured, Nanomaterials, chemistry.chemical_classification, Multidisciplinary, Vesicle, Bilayer, lcsh:R, Hydrogen Bonding, 021001 nanoscience & nanotechnology, 0104 chemical sciences, Nanostructures, chemistry, Drug delivery, Bionanotechnology, Biophysics, Medicine, lcsh:Q, Rabbits, 0210 nano-technology, Peptides, Hydrophobic and Hydrophilic Interactions, Research Article, Biotechnology |
| الوصف: | Peptide-based packaging systems show great potential as safer drug delivery systems. They overcome problems associated with lipid-based or viral delivery systems, vis-a-vis stability, specificity, inflammation, antigenicity, and tune-ability. Here, we describe a set of 15 & 23-residue branched, amphiphilic peptides that mimic phosphoglycerides in molecular architecture. These peptides undergo supramolecular self-assembly and form solvent-filled, bilayer delimited spheres with 50–200 nm diameters as confirmed by TEM, STEM and DLS. Whereas weak hydrophobic forces drive and sustain lipid bilayer assemblies, these all-peptide structures are stabilized potentially by both hydrophobic interactions and hydrogen bonds and remain intact at low micromolar concentrations and higher temperatures. A linear peptide lacking the branch point showed no self-assembly properties. We have observed that these peptide vesicles can trap fluorescent dye molecules within their interior and are taken up by N/N 1003A rabbit lens epithelial cells grown in culture. These assemblies are thus potential drug delivery systems that can overcome some of the key limitations of the current packaging systems. |
| اللغة: | English |
| تدمد: | 1932-6203 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::930438866c715d34d7a849f0113f3dfe http://europepmc.org/articles/PMC3445502?pdf=render |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....930438866c715d34d7a849f0113f3dfe |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19326203 |
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