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      Human-like smelling of a rose scent using an olfactory receptor nanodisc-based bioelectronic nose

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          Abstract

          We report a strategy for the human-like smelling of a rose scent utilizing olfactory receptor nanodisc (ND)-based bioelectronic nose devices. In this strategy, a floating electrode (FE)-based carbon nanotube (CNT) field effect transistor (FET) was functionalized with human olfactory receptor 1A2 (hOR1A2)-embedded NDs (hOR1A2NDs). The hOR1A2NDs responded to rose scent molecules specifically, which were monitored electrically using the underlying CNT-FET. This strategy allowed us to quantitatively assess the contents of geraniol and citronellol, the main components of a rose scent, as low as 1 fM and 10 fM, respectively. In addition, it enabled us to selectively discriminate a specific rose odorant from other odorants. Significantly, we also demonstrated that the responses of hOR1A2NDs to a rose scent could be strongly enhanced by enhancer materials like a human nose. Furthermore, the method provided a means to quantitatively evaluate rose scent components in real samples such as rose oil. Since our method allows one to quantitatively evaluate general rose scent ingredients just like a human nose, it could be a powerful strategy for versatile basic research and various applications such as fragrance development.

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          Most cited references55

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          Combinatorial receptor codes for odors.

          The discriminatory capacity of the mammalian olfactory system is such that thousands of volatile chemicals are perceived as having distinct odors. Here we used a combination of calcium imaging and single-cell RT-PCR to identify odorant receptors (ORs) for odorants with related structures but varied odors. We found that one OR recognizes multiple odorants and that one odorant is recognized by multiple ORs, but that different odorants are recognized by different combinations of ORs. Thus, the olfactory system uses a combinatorial receptor coding scheme to encode odor identities. Our studies also indicate that slight alterations in an odorant, or a change in its concentration, can change its "code," potentially explaining how such changes can alter perceived odor quality.
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            NanoLuc: A Small Luciferase Is Brightening Up the Field of Bioluminescence.

            The biomedical field has greatly benefited from the discovery of bioluminescent proteins. Currently, scientists employ bioluminescent systems for numerous biomedical applications, ranging from highly sensitive cellular assays to bioluminescence-based molecular imaging. Traditionally, these systems are based on Firefly and Renilla luciferases; however, the applicability of these enzymes is limited by their size, stability, and luminescence efficiency. NanoLuc (NLuc), a novel bioluminescence platform, offers several advantages over established systems, including enhanced stability, smaller size, and >150-fold increase in luminescence. In addition, the substrate for NLuc displays enhanced stability and lower background activity, opening up new possibilities in the field of bioluminescence imaging. The NLuc system is incredibly versatile and may be utilized for a wide array of applications. The increased sensitivity, high stability, and small size of the NLuc system have the potential to drastically change the field of reporter assays in the future. However, as with all such technology, NLuc has limitations (including a nonideal emission for in vivo applications and its unique substrate) which may cause it to find restricted use in certain areas of molecular biology. As this unique technology continues to broaden, NLuc may have a significant impact in both preclinical and clinical fields, with potential roles in disease detection, molecular imaging, and therapeutic monitoring. This review will present the NLuc technology to the scientific community in a nonbiased manner, allowing the audience to adopt their own views of this novel system.
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              Nanodiscs for structural and functional studies of membrane proteins.

              Membrane proteins have long presented a challenge to biochemical and functional studies. In the absence of a bilayer environment, individual proteins and critical macromolecular complexes may be insoluble and may display altered or absent activities. Nanodisc technology provides important advantages for the isolation, purification, structural resolution and functional characterization of membrane proteins. In addition, the ability to precisely control the nanodisc composition provides a nanoscale membrane surface for investigating molecular recognition events.
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                Author and article information

                Contributors
                thpark@snu.ac.kr
                seunghun@snu.ac.kr
                Journal
                Sci Rep
                Sci Rep
                Scientific Reports
                Nature Publishing Group UK (London )
                2045-2322
                17 September 2018
                17 September 2018
                2018
                : 8
                : 13945
                Affiliations
                [1 ]ISNI 0000 0004 0470 5905, GRID grid.31501.36, Department of Physics and Astronomy and Institute of Applied Physics, , Seoul National University, ; Seoul, 08826 Korea
                [2 ]ISNI 0000 0004 0470 5905, GRID grid.31501.36, School of Chemical and Biological Engineering, , Seoul National University, ; Seoul, 08826 Korea
                [3 ]Protein Engineering Laboratory, Recombinants Unit, MOGAM Institute for Biomedical Research, Yongin, 16924 Korea
                [4 ]ISNI 0000 0004 0470 5905, GRID grid.31501.36, Department of Biophysics and Chemical Biology, , Seoul National University, ; Seoul, 08826 Korea
                Author information
                http://orcid.org/0000-0002-7109-0950
                Article
                32155
                10.1038/s41598-018-32155-1
                6141559
                30224633
                9bbbf2bb-075d-40a6-801c-1cd68a5930c6
                © The Author(s) 2018

                Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

                History
                : 29 May 2018
                : 3 September 2018
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