Unknown

Dataset Information

0

Protein-assisted self-assembly of multifunctional nanoparticles.


ABSTRACT: A bioengineering method for self-assembly of multifunctional superstructures with in-advance programmable properties has been proposed. The method employs two unique proteins, barnase and barstar, to rapidly join the structural components together directly in water solutions. The properties of the superstructures can be designed on demand by linking different agents of various sizes and chemical nature, designated for specific goals. As a proof of concept, colloidally stable trifunctional structures have been assembled by binding together magnetic particles, quantum dots, and antibodies using barnase and barstar. The assembly has demonstrated that the bonds between these proteins are strong enough to hold macroscopic (5 nm-3 microm) particles together. Specific interaction of such superstructures with cancer cells resulted in fluorescent labeling of the cells and their responsiveness to magnetic field. The method can be used to join inorganic moieties, organic particles, and single biomolecules for synergistic use in different applications such as biosensors, photonics, and nanomedicine.

SUBMITTER: Nikitin MP 

PROVIDER: S-EPMC2851910 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Protein-assisted self-assembly of multifunctional nanoparticles.

Nikitin Maxim P MP   Zdobnova Tatiana A TA   Lukash Sergey V SV   Stremovskiy Oleg A OA   Deyev Sergey M SM  

Proceedings of the National Academy of Sciences of the United States of America 20100315 13


A bioengineering method for self-assembly of multifunctional superstructures with in-advance programmable properties has been proposed. The method employs two unique proteins, barnase and barstar, to rapidly join the structural components together directly in water solutions. The properties of the superstructures can be designed on demand by linking different agents of various sizes and chemical nature, designated for specific goals. As a proof of concept, colloidally stable trifunctional struct  ...[more]

Similar Datasets

| S-EPMC9237116 | biostudies-literature
| S-EPMC9419478 | biostudies-literature
2022-01-01 | GSE165635 | GEO
| S-EPMC4744166 | biostudies-literature
| S-EPMC3608202 | biostudies-literature
| S-EPMC2775065 | biostudies-literature
| S-EPMC6649285 | biostudies-literature
| S-EPMC6442733 | biostudies-literature
| S-EPMC6648767 | biostudies-literature
| S-EPMC2791182 | biostudies-literature