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Self-assembly and modular functionalization of three-dimensional crystals from oppositely charged proteins.

Liljeström V, Mikkilä J, Kostiainen MA - Nat Commun (2014)

Bottom Line: Well-developed, especially DNA-based, methods for their preparation exist, yet most techniques concentrate on molecular and synthetic nanoparticle systems in non-biocompatible environment.Here we describe the self-assembly and characterization of binary solids that consist of crystalline arrays of native biomacromolecules.Importantly, the whole preparation process takes place at room temperature in a mild aqueous medium allowing the processing of delicate biological building blocks into ordered structures with lattice constants in the nanometre range.

View Article: PubMed Central - PubMed

Affiliation: 1] Biohybrid Materials Group, Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland [2] Molecular Materials Group, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.

ABSTRACT
Multicomponent crystals and nanoparticle superlattices are a powerful approach to integrate different materials into ordered nanostructures. Well-developed, especially DNA-based, methods for their preparation exist, yet most techniques concentrate on molecular and synthetic nanoparticle systems in non-biocompatible environment. Here we describe the self-assembly and characterization of binary solids that consist of crystalline arrays of native biomacromolecules. We electrostatically assembled cowpea chlorotic mottle virus particles and avidin proteins into heterogeneous crystals, where the virus particles adopt a non-close-packed body-centred cubic arrangement held together by avidin. Importantly, the whole preparation process takes place at room temperature in a mild aqueous medium allowing the processing of delicate biological building blocks into ordered structures with lattice constants in the nanometre range. Furthermore, the use of avidin-biotin interaction allows highly selective pre- or post-functionalization of the protein crystals in a modular way with different types of functional units, such as fluorescent dyes, enzymes and plasmonic nanoparticles.

No MeSH data available.


Related in: MedlinePlus

Modular pre- and post-functionalization of CCMV–avidin crystals through biotin–avidin interaction.Method 1 and 2 describe the pre- and post-functionalization approaches, respectively.
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f5: Modular pre- and post-functionalization of CCMV–avidin crystals through biotin–avidin interaction.Method 1 and 2 describe the pre- and post-functionalization approaches, respectively.

Mentions: Avidin binds to biotin with high affinity and selectivity (Kd ~10−15 M) allowing the labelling and modular functionalization of electrostatically assembled CCMV–avidin crystals by uncharged biotin-tagged functional units (Fig. 5). In our study, we verified this by incorporating biotin (5-fluorescein) conjugate (BF), biotin-tagged horseradish peroxidase enzyme (B-HRP) and biotinylated 5 nm AuNPs (B-AuNP) into the crystal structure. The functionalization can be achieved in two ways: by pre-functionalizing avidin with the biotinylated functional unit and then adding the virus particles to form the crystals (Method 1), or by first forming the crystals followed by the addition of biotinylated agent (post-functionalization, Method 2).


Self-assembly and modular functionalization of three-dimensional crystals from oppositely charged proteins.

Liljeström V, Mikkilä J, Kostiainen MA - Nat Commun (2014)

Modular pre- and post-functionalization of CCMV–avidin crystals through biotin–avidin interaction.Method 1 and 2 describe the pre- and post-functionalization approaches, respectively.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4109007&req=5

f5: Modular pre- and post-functionalization of CCMV–avidin crystals through biotin–avidin interaction.Method 1 and 2 describe the pre- and post-functionalization approaches, respectively.
Mentions: Avidin binds to biotin with high affinity and selectivity (Kd ~10−15 M) allowing the labelling and modular functionalization of electrostatically assembled CCMV–avidin crystals by uncharged biotin-tagged functional units (Fig. 5). In our study, we verified this by incorporating biotin (5-fluorescein) conjugate (BF), biotin-tagged horseradish peroxidase enzyme (B-HRP) and biotinylated 5 nm AuNPs (B-AuNP) into the crystal structure. The functionalization can be achieved in two ways: by pre-functionalizing avidin with the biotinylated functional unit and then adding the virus particles to form the crystals (Method 1), or by first forming the crystals followed by the addition of biotinylated agent (post-functionalization, Method 2).

Bottom Line: Well-developed, especially DNA-based, methods for their preparation exist, yet most techniques concentrate on molecular and synthetic nanoparticle systems in non-biocompatible environment.Here we describe the self-assembly and characterization of binary solids that consist of crystalline arrays of native biomacromolecules.Importantly, the whole preparation process takes place at room temperature in a mild aqueous medium allowing the processing of delicate biological building blocks into ordered structures with lattice constants in the nanometre range.

View Article: PubMed Central - PubMed

Affiliation: 1] Biohybrid Materials Group, Department of Biotechnology and Chemical Technology, Aalto University, 00076 Aalto, Finland [2] Molecular Materials Group, Department of Applied Physics, Aalto University, 00076 Aalto, Finland.

ABSTRACT
Multicomponent crystals and nanoparticle superlattices are a powerful approach to integrate different materials into ordered nanostructures. Well-developed, especially DNA-based, methods for their preparation exist, yet most techniques concentrate on molecular and synthetic nanoparticle systems in non-biocompatible environment. Here we describe the self-assembly and characterization of binary solids that consist of crystalline arrays of native biomacromolecules. We electrostatically assembled cowpea chlorotic mottle virus particles and avidin proteins into heterogeneous crystals, where the virus particles adopt a non-close-packed body-centred cubic arrangement held together by avidin. Importantly, the whole preparation process takes place at room temperature in a mild aqueous medium allowing the processing of delicate biological building blocks into ordered structures with lattice constants in the nanometre range. Furthermore, the use of avidin-biotin interaction allows highly selective pre- or post-functionalization of the protein crystals in a modular way with different types of functional units, such as fluorescent dyes, enzymes and plasmonic nanoparticles.

No MeSH data available.


Related in: MedlinePlus