Protein-assisted self-assembly of multifunctional nanoparticles

Maxim P. Nikitin, Tatiana A. Zdobnova, Sergey V. Lukash, Oleg A. Stremovskiy, Sergey M. Deyev

Research output: Contribution to journalArticle

71 Citations (Scopus)

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 μm) 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.

Original languageEnglish
Pages (from-to)5827-5832
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume107
Issue number13
DOIs
Publication statusPublished - 30 Mar 2010
Externally publishedYes

Keywords

  • Cancer cells
  • Fusion proteins
  • Magnetic nanoparticles
  • Superstructures
  • Targeting

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Protein-assisted self-assembly of multifunctional nanoparticles'. Together they form a unique fingerprint.

  • Cite this