Fusogenic Liposomes as Nanocarriers for the Delivery of Intracellular Proteins. 2017

Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár

Direct delivery of proteins and peptides into living mammalian cells has been accomplished using phospholipid liposomes as carrier particles. Such liposomes are usually taken up via endocytosis where the main part of their cargo is degraded in lysosomes before reaching its destination. Here, fusogenic liposomes, a newly developed molecular carrier system, were used for protein delivery. When such liposomes were loaded with water-soluble proteins and brought into contact with mammalian cells, the liposomal membrane efficiently fused with the cellular plasma membrane delivering the liposomal content to the cytoplasm without degradation. To explore the key factors of proteofection processes, the complex formation of fusogenic liposomes and proteins of interest and the size and zeta potential of the formed fusogenic proteoliposoms were monitored. Intracellular protein delivery was analyzed using fluorescence microscopy and flow cytometry. Proteins such as EGFP, Dendra2, and R-phycoerythrin or peptides such as LifeAct-FITC and NTF2-AlexaFluor488 were successfully incorporated into mammalian cells with high efficiency. Moreover, correct functionality and faithful transport to binding sites were also proven for the imported proteins.

UI MeSH Term Description Entries
D008081 Liposomes Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins. Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D003412 Cricetulus A genus of the family Muridae consisting of eleven species. C. migratorius, the grey or Armenian hamster, and C. griseus, the Chinese hamster, are the two species used in biomedical research. Hamsters, Armenian,Hamsters, Chinese,Hamsters, Grey,Armenian Hamster,Armenian Hamsters,Chinese Hamster,Chinese Hamsters,Grey Hamster,Grey Hamsters,Hamster, Armenian,Hamster, Chinese,Hamster, Grey
D003593 Cytoplasm The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990) Protoplasm,Cytoplasms,Protoplasms
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D016466 CHO Cells CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells. CHO Cell,Cell, CHO,Cells, CHO
D021381 Protein Transport The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport. Cellular Protein Targeting,Gated Protein Transport,Protein Targeting, Cellular,Protein Translocation,Transmembrane Protein Transport,Vesicular Protein Transport,Protein Localization Processes, Cellular,Protein Sorting,Protein Trafficking,Protein Transport, Gated,Protein Transport, Transmembrane,Protein Transport, Vesicular,Traffickings, Protein

Related Publications

Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
January 2021, International journal of molecular sciences,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
January 2010, Methods in molecular biology (Clifton, N.J.),
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
May 2007, Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
June 2017, Journal of controlled release : official journal of the Controlled Release Society,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
April 2017, Nanomedicine (London, England),
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
November 2001, Advanced drug delivery reviews,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
November 2023, Biomaterials,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
September 2017, Biomaterials,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
July 2011, Chemical Society reviews,
Sarah Kube, and Nils Hersch, and Elena Naumovska, and Thomas Gensch, and Johnny Hendriks, and Arne Franzen, and Lisa Landvogt, and Jan-Peter Siebrasse, and Ulrich Kubitscheck, and Bernd Hoffmann, and Rudolf Merkel, and Agnes Csiszár
December 2017, Biophysical reviews,
Copied contents to your clipboard!