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Title: Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration

Abstract

We developed membrane voltage nanosensors that are based on inorganic semiconductor nanoparticles. We provide here a feasibility study for their utilization. We use a rationally designed peptide to functionalize the nanosensors, imparting them with the ability to self-insert into a lipid membrane with a desired orientation. Once inserted, these nanosensors could sense membrane potential via the quantum confined Stark effect, with a single-particle sensitivity. With further improvements, these nanosensors could potentially be used for simultaneous recording of action potentials from multiple neurons in a large field of view over a long duration and for recording electrical signals on the nanoscale, such as across one synapse.

Authors:
 [1]; ORCiD logo [1]; ORCiD logo [2]; ORCiD logo [1];  [3]; ORCiD logo [4];  [5]; ORCiD logo [6];  [7];  [8];  [1]; ORCiD logo [9]
+ Show Author Affiliations
  1. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry
  2. Academy of Sciences of the Czech Republic (ASCR), Prague (Czech Republic). Inst. of Organic Chemistry and Biochemistry
  3. Univ. of California, Los Angeles, CA (United States). Dept. of Microbiology, Immunology, and Molecular Genetics
  4. Univ. of California, Los Angeles, CA (United States). Dept. of Chemical and Biomolecular Engineering
  5. Univ. of California, Los Angeles, CA (United States). Dept. of Ecology and Evolutionary Biology
  6. Univ. of California, Los Angeles, CA (United States). Dept. of Microbiology, Immunology, and Molecular Genetics. California NanoSystems Inst.
  7. Harvard Univ., Cambridge, MA (United States). Dept. of Chemistry and Chemical Biology
  8. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry. Dept. of Physics
  9. Univ. of California, Los Angeles, CA (United States). Dept. of Chemistry and Biochemistry. California NanoSystems Inst. Dept. of Physiology
Publication Date:
Research Org.:
Univ. of California, Los Angeles, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States); National Science Foundation (NSF); Defense Advanced Research Projects Agency (DARPA) (United States); United States–Israel Binational Science Foundation; Human Frontier Science Program
OSTI Identifier:
1499965
Grant/Contract Number:  
FC02-02ER63421; AC02-05CH11231; 1S10RR23057; GM071940; DMR-1309188; DMR-1548924; D14PC00141; 2010382; RGP0061/2015
Resource Type:
Accepted Manuscript
Journal Name:
Science Advances
Additional Journal Information:
Journal Volume: 4; Journal Issue: 1; Journal ID: ISSN 2375-2548
Publisher:
AAAS
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; 36 MATERIALS SCIENCE

Citation Formats

Park, Kyoungwon, Kuo, Yung, Shvadchak, Volodymyr, Ingargiola, Antonino, Dai, Xinghong, Hsiung, Lawrence, Kim, Wookyeom, Zhou, Hong, Zou, Peng, Levine, Alex J., Li, Jack, and Weiss, Shimon. Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration. United States: N. p., 2018. Web. doi:10.1126/sciadv.1601453.
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Park, Kyoungwon, Kuo, Yung, Shvadchak, Volodymyr, Ingargiola, Antonino, Dai, Xinghong, Hsiung, Lawrence, Kim, Wookyeom, Zhou, Hong, Zou, Peng, Levine, Alex J., Li, Jack, & Weiss, Shimon. Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration. United States. doi:10.1126/sciadv.1601453.
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Park, Kyoungwon, Kuo, Yung, Shvadchak, Volodymyr, Ingargiola, Antonino, Dai, Xinghong, Hsiung, Lawrence, Kim, Wookyeom, Zhou, Hong, Zou, Peng, Levine, Alex J., Li, Jack, and Weiss, Shimon. Fri . "Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration". United States. doi:10.1126/sciadv.1601453. https://www.osti.gov/servlets/purl/1499965.
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@article{osti_1499965,
title = {Membrane insertion of—and membrane potential sensing by—semiconductor voltage nanosensors: Feasibility demonstration},
author = {Park, Kyoungwon and Kuo, Yung and Shvadchak, Volodymyr and Ingargiola, Antonino and Dai, Xinghong and Hsiung, Lawrence and Kim, Wookyeom and Zhou, Hong and Zou, Peng and Levine, Alex J. and Li, Jack and Weiss, Shimon},
abstractNote = {We developed membrane voltage nanosensors that are based on inorganic semiconductor nanoparticles. We provide here a feasibility study for their utilization. We use a rationally designed peptide to functionalize the nanosensors, imparting them with the ability to self-insert into a lipid membrane with a desired orientation. Once inserted, these nanosensors could sense membrane potential via the quantum confined Stark effect, with a single-particle sensitivity. With further improvements, these nanosensors could potentially be used for simultaneous recording of action potentials from multiple neurons in a large field of view over a long duration and for recording electrical signals on the nanoscale, such as across one synapse.},
doi = {10.1126/sciadv.1601453},
journal = {Science Advances},
number = 1,
volume = 4,
place = {United States},
year = {2018},
month = {1}
}
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Journal Article:
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DOI:  10.1126/sciadv.1601453
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Cited by: 13 works
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Figures / Tables:

Fig. 1. Fig. 1.: Surface functionalization. (A) Cartoon describing design principles for rendering NR membrane protein–like properties. This functionalization will favor their stable, spontaneous insertion into the membrane with the correct orientation. (B) Peptide design for implementing (A). (C) Top view of an NR coated with peptides. Brown and orange colors depictmore » Cys-rich and lipophilic faces of the α-helical peptide, respectively. (D) Sequence of the designed peptide. C14-CO- stands for myristoyl acid residue attached to the N-terminal amino group. (E) Wheel diagram corresponding to the a-helical part of the peptide. Color coding is the same as in (C). aa, amino acid.« less
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