J2-2131 — Annual report 2011
1.
Self-assembling polypeptide polyhedra

The invention relates to polypeptides capable of forming polyhedra by self-assembly. The polypeptide is composed of at least 12 coiled-coil-forming segments connected via linker segments, wherein each of the edges of the polyhedron is constructed of a pair of said coiled-coil-forming segments. We described the design and process for preparation of self-assembling tetrahedron, the simplest polyhedron. Polypeptide chain comprising 12 coiled-coil-forming segments in a defined order was succesfully assembled into tetrahedron. The nanostructure was characterized using different methods.

F.33 Slovenian patent

COBISS.SI-ID: 35592197
2.
Design of self-assembling polypeptide tetrahedron

We designed the tetrahedron that self-assembles from a single polypeptide chain comprising 12 concatenated coiled-coil-forming peptide segments separated by flexible peptide hinges. Self-assembling of the recombinat polypeptide is defined by the precise order of coiled-coil-forming segments and their pairwise interactions that form 6 rigid edges, each measuring approx. 5 nm. We characterized the obtained nanostructure using different methods, transmission electron microscopy, atomic force microscopy, dynamic light scattering. Split fluorescent protein attached to the termini of the polypeptide is reconstituted only by the correctly formed tetrahedron, while polypeptides with a deleted or scrambled segment order fail to self-assemble correctly.

B.04 Guest lecture

COBISS.SI-ID: 4911642
3.
Self-assembly of polypeptides into nanoscale structures

We demonstrated the principle of self-assembling polypeptide nanostructure design. We presented the tetrahedron that self-assembles from a single polypeptide chain comprising 12 concatenated coiled-coil-forming peptide segments separated by flexible peptide hinges. Self-assembling of the recombinat polypeptide is defined by the precise order of coiled-coil-forming segments and their pairwise interactions that form 6 rigid edges, each measuring approx. 5 nm. We characterized the obtained nanostructure using different methods, transmission electron microscopy, atomic force microscopy, dynamic light scattering. Split fluorescent protein attached to the termini of the polypeptide is reconstituted only by the correctly formed tetrahedron, while polypeptides with a deleted or scrambled segment order fail to self-assemble correctly.

B.04 Guest lecture

COBISS.SI-ID: 4827162