DNA Origami Meets Polymers: A Powerful Tool for the Design of Defined Nanostructures

Hannewald, Nadine; Winterwerber, Pia; Zechel, Stefan; Ng, David Y. W.; Hager, Martin D.; Weil, Tanja; Schubert, Ulrich S.

doi:10.1002/anie.202005907

“…The combination of a highly structured HTHP protein platform with short, adaptable DNA sequences leads to an advanced level of biomimicry with great modular control. [34] Via the protein platform the number and structural organization of the recruited proteins can be controlled and DNA recruitment domains allow tuning of affinity and dynamics. The presented system and general concept are expected to enable diverse bottom-up approaches for protein assembly and control of enzyme activation.…”

Section: Angewandte Chemiementioning

confidence: 99%

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains

Mashima

¹

,

Rosier

²

,

Oohora

³

et al. 2021

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Hexameric hemoprotein (HTHP) is employed as a scaffold protein for the supramolecular assembly and activation of the apoptotic signalling enzyme caspase‐9, using short DNA elements as modular recruitment domains. Caspase‐9 assembly and activation on the HTHP platform due to enhanced proximity is followed by combinatorial inhibition at high scaffold concentrations. The DNA recruitment domains allow for reversible switching of the caspase‐9 assembly and activity state using short modulatory DNA strands. Tuning of the recruitment domain affinity allows for generating kinetically trapped active enzyme complexes, as well as for dynamic repositioning of caspases over scaffold populations and inhibition using monovalent sink platforms. The conceptual combination of a highly structured multivalent protein platform with modular DNA recruitment domains provides emergent biomimicry properties with advanced levels of control over protein assembly.

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“…The combination of a highly structured HTHP protein platform with short, adaptable DNA sequences leads to an advanced level of biomimicry with great modular control. [34] Via the protein platform the number and structural organization of the recruited proteins can be controlled and DNA recruitment domains allow tuning of affinity and dynamics. The presented system and general concept are…”

Section: Angewandte Chemiementioning

confidence: 99%

“…This study has highlighted the potential of combining protein‐based scaffolds with DNA‐based recruitment elements for the generation and study of higher‐ordered enzyme assemblies. The combination of a highly structured HTHP protein platform with short, adaptable DNA sequences leads to an advanced level of biomimicry with great modular control [34] . Via the protein platform the number and structural organization of the recruited proteins can be controlled and DNA recruitment domains allow tuning of affinity and dynamics.…”

Section: Figurementioning

confidence: 99%

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains

Mashima

¹

,

Rosier

²

,

Oohora

³

et al. 2021

View full text Add to dashboard Cite

Hexameric hemoprotein (HTHP) is employed as a scaffold protein for the supramolecular assembly and activation of the apoptotic signalling enzyme caspase‐9, using short DNA elements as modular recruitment domains. Caspase‐9 assembly and activation on the HTHP platform due to enhanced proximity is followed by combinatorial inhibition at high scaffold concentrations. The DNA recruitment domains allow for reversible switching of the caspase‐9 assembly and activity state using short modulatory DNA strands. Tuning of the recruitment domain affinity allows for generating kinetically trapped active enzyme complexes, as well as for dynamic repositioning of caspases over scaffold populations and inhibition using monovalent sink platforms. The conceptual combination of a highly structured multivalent protein platform with modular DNA recruitment domains provides emergent biomimicry properties with advanced levels of control over protein assembly.

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“…Rational design of DNA nanostructures, and in particular DNA origami‐based structures, enables controlled nanoscale organization of a large number of molecular species, [20, 21] including metal nanoparticles with tunable optical properties, [22] seeded growth of gold nanostructures, [23] and shape‐controlled synthesis of covalent polymers [24] . The combination of DNA nanotechnology and covalent polymers has resulted in a new class of hybrid materials [25] with exciting properties through templated routing [26] . Manipulation of the nanoscale patterning of individual DNA‐conjugated synthetic polymers on a DNA origami platform offers exciting possibilities for polymer nanosynthesis [27] .…”

Section: Figurementioning

confidence: 99%

Assembly of Dynamic Supramolecular Polymers on a DNA Origami Platform

Schill

¹

,

Rosier

²

,

Gumí-Audenis

³

et al. 2021

Angewandte Chemie

0

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Biological processes rely on transient interactions that govern assembly of biomolecules into higher order, multi‐component systems. A synthetic platform for the dynamic assembly of multicomponent complexes would provide novel entries to study and modulate the assembly of artificial systems into higher order topologies. Here, we establish a hybrid DNA origami‐based approach as an assembly platform that enables dynamic templating of supramolecular architectures. It entails the site‐selective recruitment of supramolecular polymers to the platform with preservation of the intrinsic dynamics and reversibility of the assembly process. The composition of the supramolecular assembly on the platform can be tuned dynamically, allowing for monomer rearrangement and inclusion of molecular cargo. This work should aid the study of supramolecular structures in their native environment in real‐time and incites new strategies for controlled multicomponent self‐assembly of synthetic building blocks.

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DNA Origami Meets Polymers: A Powerful Tool for the Design of Defined Nanostructures

Abstract: Figure 7. "Brush-" and "block-type" peptoids should lead to different surface coatings on octahedra-shaped DNA origami. Reprinted from Ref. [35] with permission.

Cited by 36 publications

References 52 publications

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains

Dynamic Protease Activation on a Multimeric Synthetic Protein Scaffold via Adaptable DNA‐Based Recruitment Domains

Assembly of Dynamic Supramolecular Polymers on a DNA Origami Platform

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