Colloidal stability: Versus self-assembly of nanoparticles controlled by coiled-coil protein interactions

Allison Siehr; Bin Xu; Ronald A. Siegel; Wei Shen

doi:10.1039/c9sm01314h

Colloidal stability: Versus self-assembly of nanoparticles controlled by coiled-coil protein interactions

Allison Siehr, Bin Xu, Ronald A. Siegel, Wei Shen

Research output: Contribution to journal › Article › peer-review

Abstract

Orientational discrimination of biomolecular recognition is exploited here as a molecular engineering tool to regulate nanoparticle self-assembly or stability. Nanoparticles are conjugated with the heterodimerizing coiled-coils, A and B, which associate in parallel orientation. Simply flipping the orientation of one coiled-coil results in either self-assembling or colloidally stable nanoparticles.

Original language	English (US)
Pages (from-to)	7122-7126
Number of pages	5
Journal	Soft Matter
Volume	15
Issue number	36
DOIs	https://doi.org/10.1039/c9sm01314h
State	Published - 2019

Bibliographical note

Funding Information:
This project was supported by funds from the National Science Foundation (NSF) Career Award DMR-1151529, the University of Minnesota Institute for Engineering in Medicine, the University of Minnesota Academic Health Center, and the University of Minnesota Industrial Partnership for Research in Interfacial and Materials Engineering (IPRIME). A. S. was supported by a Biotechnology Training Grant (NIH T32GM008347) and the Institute for Molecular Virology Training Program (NIH T32 AI83196). Parts of this work were carried out in the Characterization Facility at the University of Minnesota, which receives partial support from NSF through the MRSEC program.

Publisher Copyright:
© The Royal Society of Chemistry.

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title = "Colloidal stability: Versus self-assembly of nanoparticles controlled by coiled-coil protein interactions",

abstract = "Orientational discrimination of biomolecular recognition is exploited here as a molecular engineering tool to regulate nanoparticle self-assembly or stability. Nanoparticles are conjugated with the heterodimerizing coiled-coils, A and B, which associate in parallel orientation. Simply flipping the orientation of one coiled-coil results in either self-assembling or colloidally stable nanoparticles.",

author = "Allison Siehr and Bin Xu and Siegel, {Ronald A.} and Wei Shen",

note = "Funding Information: This project was supported by funds from the National Science Foundation (NSF) Career Award DMR-1151529, the University of Minnesota Institute for Engineering in Medicine, the University of Minnesota Academic Health Center, and the University of Minnesota Industrial Partnership for Research in Interfacial and Materials Engineering (IPRIME). A. S. was supported by a Biotechnology Training Grant (NIH T32GM008347) and the Institute for Molecular Virology Training Program (NIH T32 AI83196). Parts of this work were carried out in the Characterization Facility at the University of Minnesota, which receives partial support from NSF through the MRSEC program. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry.",

year = "2019",

doi = "10.1039/c9sm01314h",

language = "English (US)",

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pages = "7122--7126",

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AU - Siegel, Ronald A.

AU - Shen, Wei

N1 - Funding Information: This project was supported by funds from the National Science Foundation (NSF) Career Award DMR-1151529, the University of Minnesota Institute for Engineering in Medicine, the University of Minnesota Academic Health Center, and the University of Minnesota Industrial Partnership for Research in Interfacial and Materials Engineering (IPRIME). A. S. was supported by a Biotechnology Training Grant (NIH T32GM008347) and the Institute for Molecular Virology Training Program (NIH T32 AI83196). Parts of this work were carried out in the Characterization Facility at the University of Minnesota, which receives partial support from NSF through the MRSEC program. Publisher Copyright: © The Royal Society of Chemistry.

PY - 2019

Y1 - 2019

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Colloidal stability: Versus self-assembly of nanoparticles controlled by coiled-coil protein interactions

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