Synthetic Virus-Like Particles from Self-Assembling Coiled-Coil Lipopeptides and Their Use in Antigen Display to the Immune System

2007 ◽  
Vol 119 (47) ◽  
pp. 9173-9176 ◽  
Author(s):  
Francesca Boato ◽  
Richard M. Thomas ◽  
Arin Ghasparian ◽  
Annabelle Freund-Renard ◽  
Kerstin Moehle ◽  
...  
Keyword(s):  
Immune System ◽  
Coiled Coil ◽  
Virus Like Particles ◽  
Self Assembling

Synthetic Virus-Like Particles from Self-Assembling Coiled-Coil Lipopeptides and Their Use in Antigen Display to the Immune System

2007 ◽  
Vol 46 (47) ◽  
pp. 9015-9018 ◽  
Author(s):  
Francesca Boato ◽  
Richard M. Thomas ◽  
Arin Ghasparian ◽  
Annabelle Freund-Renard ◽  
Kerstin Moehle ◽  
...  
Keyword(s):  
Immune System ◽  
Coiled Coil ◽  
Virus Like Particles ◽  
Self Assembling

scholarly journals Coiled-Coils: The Molecular Zippers that Self-Assemble Protein Nanostructures

2020 ◽  
Vol 21 (10) ◽  
pp. 3584 ◽  
Author(s):  
Won Min Park
Keyword(s):  
Modular Design ◽  
Coiled Coil ◽  
Molecular Complexes ◽  
Building Blocks ◽  
Structural Features ◽  
Coiled Coils ◽  
Design Strategies ◽  
Protein Motifs ◽  
Self Assembling ◽  
Current Design

Coiled-coils, the bundles of intertwined helical protein motifs, have drawn much attention as versatile molecular toolkits. Because of programmable interaction specificity and affinity as well as well-established sequence-to-structure relationships, coiled-coils have been used as subunits that self-assemble various molecular complexes in a range of fields. In this review, I describe recent advances in the field of protein nanotechnology, with a focus on programming assembly of protein nanostructures using coiled-coil modules. Modular design approaches to converting the helical motifs into self-assembling building blocks are described, followed by a discussion on the molecular basis and principles underlying the modular designs. This review also provides a summary of recently developed nanostructures with a variety of structural features, which are in categories of unbounded nanostructures, discrete nanoparticles, and well-defined origami nanostructures. Challenges existing in current design strategies, as well as desired improvements for controls over material properties and functionalities for applications, are also provided.

scholarly journals The use of a P. falciparum specific coiled-coil domain to construct a self-assembling protein nanoparticle vaccine to prevent malaria

2017 ◽  
Vol 15 (1) ◽  
Author(s):  
Christopher P. Karch ◽  
Tais A. P. F. Doll ◽  
Sara M. Paulillo ◽  
Issa Nebie ◽  
David E. Lanar ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Self Assembling ◽  
Coiled Coil Domain

scholarly journals Self-Assembling Cages from Coiled-Coil Peptide Modules

Science ◽  
2013 ◽  
Vol 340 (6132) ◽  
pp. 595-599 ◽  
Author(s):  
J. M. Fletcher ◽  
R. L. Harniman ◽  
F. R. H. Barnes ◽  
A. L. Boyle ◽  
A. Collins ◽  
...  
Keyword(s):  
Coiled Coil ◽  
Self Assembling

scholarly journals Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint

2013 ◽  
Vol 14 (2) ◽  
pp. 2788-2807 ◽  
Author(s):  
John Young ◽  
Benjamin Clayton ◽  
Alexandra Kikonyogo ◽  
Truc-Chi Pham ◽  
Abby Parrill
Keyword(s):  
Structural Characterization ◽  
Coiled Coil ◽  
Extracellular Loop ◽  
Self Assembling

Hierarchical Assembly of DNA Origami Nanostructures Using Coiled-coil Peptides

2019 ◽  
Author(s):  
Alex Buchberger ◽  
Chad Simmons ◽  
Nour Fahmi ◽  
Ronit Freeman ◽  
Nicholas Stephanopoulos
Keyword(s):  
Self Assembly ◽  
Coiled Coil ◽  
Dna Origami ◽  
Hybrid Nanostructures ◽  
Hierarchical Assembly ◽  
Alternating Copolymer ◽  
Self Assembling ◽  
Potential Applications ◽  
Multiple Routes ◽  
Stepwise Assembly

DNA and peptides are two of the most commonly used biomolecules for building self-assembling materials, but few examples exist of hybrid nanostructures that contain both components. Here we report the modification of two peptides that comprise a coiled-coil heterodimer pair with orthogonal DNA handles in order to link DNA origami nanostructures bearing complementary strands into micrometer long one-dimensional arrays. We probed the effect of number of coils on self-assembly and demonstrated the formation of self-assembled structures through multiple routes, to form dimers and trimers, an alternating copolymer of two different origami bundles, and stepwise assembly of purified structures with coiled-coil conjugates. Our results demonstrate the successful merging of two distinct self-assembly modes to create hybrid bionanomaterials expected to have a range of potential applications in the future.

Functional self-assembling polypeptide bionanomaterials

2012 ◽  
Vol 40 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Tibor Doles ◽  
Sabina Božič ◽  
Helena Gradišar ◽  
Roman Jerala
Keyword(s):  
Self Assembly ◽  
Biological Systems ◽  
Three Dimensional ◽  
Coiled Coil ◽  
Chemical Properties ◽  
Building Blocks ◽  
External Signal ◽  
Form Complex ◽  
Cell Factories ◽  
Self Assembling

Bionanotechnology seeks to modify and design new biopolymers and their applications and uses biological systems as cell factories for the production of nanomaterials. Molecular self-assembly as the main organizing principle of biological systems is also the driving force for the assembly of artificial bionanomaterials. Protein domains and peptides are particularly attractive as building blocks because of their ability to form complex three-dimensional assemblies from a combination of at least two oligomerization domains that have the oligomerization state of at least two and three respectively. In the present paper, we review the application of polypeptide-based material for the formation of material with nanometre-scale pores that can be used for the separation. Use of antiparallel coiled-coil dimerization domains introduces the possibility of modulation of pore size and chemical properties. Assembly or disassembly of bionanomaterials can be regulated by an external signal as demonstrated by the coumermycin-induced dimerization of the gyrase B domain which triggers the formation of polypeptide assembly.

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