Product name
Nanovesicle Forming, Self-Assembling Functional PeptidesSummary
encapsulation of bioactive compounds and their environmentally induced release (e.g. targeted drug delivery), the use as vaccine carriers due to attached polysaccharidesOrganization name
University of BaselProfile
Amphiphilic peptides can self-assemble in aqueous media into well-defined supramolecular aggregates similar to more conventional low molar mass or macromolecular amphiphiles. The present amphiphilic peptides are inspired by the antibiotic gramicidin A. These peptides reversibly self-assemble in aqueous media into vesicular structures with diameters around 200 to 300 nm.
Electron microscopical, atomic force microscopical (AFM), light scattering and circular dichroism spectroscopical investigations reveal that the wall forming peptide membranes have an extraordinary high mechanical stability. Moreover, our experiments reveal that self-assembly in these systems is not only controlled by the amphiphilic nature of the peptides but also by their well-defined secondary and quaternary structure. Due to the peptidic architecture functionalities can easily be introduced and adapted to external needs.
Advantages
- a highly tunable functionality due to the peptidic architecture
- a responsive system due to chances in peptidic secondary and quaternary structure (e.g. induced by pH or ion strength)
- switchable bioactivity or targeting due to attachable signal molecules or receptors (peptides or polysaccharides)
- possibly controllable immune response (vaccine)
- compatible with lipid membranes
- high antibiotic potential due to the gramicidin channels
- short peptide but full features of long proteins (highly folded secondary structure and specific dimerization behavior)
- potential for ion uptake/release due to the cation-selective gramicidin channel
- various adaptable functionalities due to straightforward linking to further amino acid residues.
Applications
Possible applications are the encapsulation of bioactive compounds and their environmentally induced release (e.g. targeted drug delivery), the use as vaccine carriers due to attached polysaccharides. Furthermore, on hybridization on surfaces (dimer), regenerative functionalization as used in biosensors could be envisaged. Due to the selectivity of the Gramicidin channels to monovalent cations, encapsulation of analytical receptors to detect monovalent cations in difficult matrices may be an additional field of application. There is also seen a high potential for the usage as an antibiotic in the antibiotic/antibacterial treatment of surfaces.
Contact
Mathias Weiss
mathias.weiss(at)unibas.ch
About University Basel
The University of Basel was founded in 1460. It is the oldest university in Switzerland. Located in the heart of Basel, and drawing on innovation anchored in tradition, the University of Basel is dynamic and innovative. They offer a broad range of attractive undergraduate and postgraduate programmes, access to reputable international research networks, and provide a wide range of services to students and the community. The University of Basel is committed to providing state-of-the-art education and to facilitating outstanding research. Their key strategic aim is to develop, enhance, and sponsor research which has acknowledged standards of excellence, and to provide an atmosphere and infrastructure commensurate with that objective.
Description File
InventionProfileSummary_07-205.pdf
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