Designer Amyloid Cell-Penetrating Peptides for Potential Use as Gene Transfer Vehicles
| Autor: | Asuka A. Orr, Sai Vamshi R. Jonnalagadda, And Anna Mitraki, Chrysoula Kokotidou, Phanourios Tamamis, Androniki Kretsovali, George Vrentzos |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Amyloid
media_common.quotation_subject Cell Peptide Cell-Penetrating Peptides 02 engineering and technology scaffold DNA condensation Fibril medicine.disease_cause Biochemistry Article 03 medical and health sciences computational biology Escherichia coli medicine gene transfer Internalization Enhancer Molecular Biology 030304 developmental biology media_common chemistry.chemical_classification 0303 health sciences Chemistry Gene Transfer Techniques amyloid 021001 nanoscience & nanotechnology molecular dynamics peptide medicine.anatomical_structure Biophysics Protein Conformation beta-Strand 0210 nano-technology Plasmids |
| Zdroj: | Biomolecules Volume 10 Issue 1 |
| ISSN: | 2218-273X |
| DOI: | 10.3390/biom10010007 |
| Popis: | Cell-penetrating peptides are used extensively to deliver molecules into cells due to their unique characteristics such as rapid internalization, charge, and non-cytotoxicity. Amyloid fibril biomaterials were reported as gene transfer or retroviral infection enhancers no cell internalization of the peptides themselves is reported so far. In this study, we focus on two rationally and computationally designed peptides comprised of &beta sheet cores derived from naturally occurring protein sequences and designed positively charged and aromatic residues exposed at key residue positions. The &beta sheet cores bestow the designed peptides with the ability to self-assemble into amyloid fibrils. The introduction of positively charged and aromatic residues additionally promotes DNA condensation and cell internalization by the self-assembled material formed by the designed peptides. Our results demonstrate that these designer peptide fibrils can efficiently enter mammalian cells while carrying packaged luciferase-encoding plasmid DNA, and they can act as a protein expression enhancer. Interestingly, the peptides additionally exhibited strong antimicrobial activity against the enterobacterium Escherichia coli. |
| Databáze: | OpenAIRE |
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