2
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Single-Molecule Sizing through Nanocavity Confinement

      rapid-communication

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          An approach relying on nanocavity confinement is developed in this paper for the sizing of nanoscale particles and single biomolecules in solution. The approach, termed nanocavity diffusional sizing (NDS), measures particle residence times within nanofluidic cavities to determine their hydrodynamic radii. Using theoretical modeling and simulations, we show that the residence time of particles within nanocavities above a critical time scale depends on the diffusion coefficient of the particle, which allows the estimation of the particle’s size. We demonstrate this approach experimentally through the measurement of particle residence times within nanofluidic cavities using single-molecule confocal microscopy. Our data show that the residence times scale linearly with the sizes of nanoscale colloids, protein aggregates, and single DNA oligonucleotides. NDS thus constitutes a new single molecule optofluidic approach that allows rapid and quantitative sizing of nanoscale particles for potential applications in nanobiotechnology, biophysics, and clinical diagnostics.

          Related collections

          Most cited references31

          • Record: found
          • Abstract: found
          • Article: not found

          Critical Evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the Measurement of Nanoparticles and Protein Aggregates

          Purpose To evaluate the nanoparticle tracking analysis (NTA) technique, compare it with dynamic light scattering (DLS) and test its performance in characterizing drug delivery nanoparticles and protein aggregates. Methods Standard polystyrene beads of sizes ranging from 60 to 1,000 nm and physical mixtures thereof were analyzed with NTA and DLS. The influence of different ratios of particle populations was tested. Drug delivery nanoparticles and protein aggregates were analyzed by NTA and DLS. Live monitoring of heat-induced protein aggregation was performed with NTA. Results NTA was shown to accurately analyze the size distribution of monodisperse and polydisperse samples. Sample visualization and individual particle tracking are features that enable a thorough size distribution analysis. The presence of small amounts of large (1,000 nm) particles generally does not compromise the accuracy of NTA measurements, and a broad range of population ratios can easily be detected and accurately sized. NTA proved to be suitable to characterize drug delivery nanoparticles and protein aggregates, complementing DLS. Live monitoring of heat-induced protein aggregation provides information about aggregation kinetics and size of submicron aggregates. Conclusion NTA is a powerful characterization technique that complements DLS and is particularly valuable for analyzing polydisperse nanosized particles and protein aggregates.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            The amyloid state and its association with protein misfolding diseases.

            The phenomenon of protein aggregation and amyloid formation has become the subject of rapidly increasing research activities across a wide range of scientific disciplines. Such activities have been stimulated by the association of amyloid deposition with a range of debilitating medical disorders, from Alzheimer's disease to type II diabetes, many of which are major threats to human health and welfare in the modern world. It has become clear, however, that the ability to form the amyloid state is more general than previously imagined, and that its study can provide unique insights into the nature of the functional forms of peptides and proteins, as well as understanding the means by which protein homeostasis can be maintained and protein metastasis avoided.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Dynamic light scattering: a practical guide and applications in biomedical sciences.

              Dynamic light scattering (DLS), also known as photon correlation spectroscopy (PCS), is a very powerful tool for studying the diffusion behaviour of macromolecules in solution. The diffusion coefficient, and hence the hydrodynamic radii calculated from it, depends on the size and shape of macromolecules. In this review, we provide evidence of the usefulness of DLS to study the homogeneity of proteins, nucleic acids, and complexes of protein-protein or protein-nucleic acid preparations, as well as to study protein-small molecule interactions. Further, we provide examples of DLS's application both as a complementary method to analytical ultracentrifugation studies and as a screening tool to validate solution scattering models using determined hydrodynamic radii.
                Bookmark

                Author and article information

                Journal
                Nano Lett
                Nano Lett
                nl
                nalefd
                Nano Letters
                American Chemical Society
                1530-6984
                1530-6992
                24 February 2023
                08 March 2023
                : 23
                : 5
                : 1629-1636
                Affiliations
                []Yusuf Hamied Department of Chemistry, University of Cambridge , Lensfield Road, Cambridge, CB2 1EW, United Kingdom
                []Department of Chemical Engineering and Biotechnology, University of Cambridge , Philippa Fawcett Drive, Cambridge CB3 0AS, United Kingdom
                [§ ]Cavendish Laboratory, Department of Physics, University of Cambridge , J. J. Thomson Avenue, Cambridge CB3 0HE, United Kingdom
                []Department of Physics and Technology, UiT The Arctic University of Norway , Technology Building, Klokkargårdsbakken 35, 9019 Tromsø, Norway
                Author notes
                Author information
                https://orcid.org/0000-0002-8661-9722
                https://orcid.org/0000-0002-9626-7636
                https://orcid.org/0000-0002-8018-3059
                https://orcid.org/0000-0002-5708-9726
                https://orcid.org/0000-0001-5611-470X
                https://orcid.org/0000-0003-4726-636X
                https://orcid.org/0000-0001-7817-5722
                https://orcid.org/0000-0002-5194-0962
                https://orcid.org/0000-0003-3188-5414
                https://orcid.org/0000-0002-9606-9488
                https://orcid.org/0000-0002-7879-0140
                Article
                10.1021/acs.nanolett.1c04830
                9999452
                36826991
                a7977f2c-004d-4293-a38f-9e4cdf3fb787
                © 2023 The Authors. Published by American Chemical Society

                Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained ( https://creativecommons.org/licenses/by/4.0/).

                History
                : 14 December 2021
                : 16 February 2023
                Funding
                Funded by: H2020 Future and Emerging Technologies, doi 10.13039/100010664;
                Award ID: 766972
                Funded by: Engineering and Physical Sciences Research Council, doi 10.13039/501100000266;
                Award ID: EP/L015889/1
                Funded by: Marie Sklodowska-Curie Actions, doi 10.13039/100018694;
                Award ID: 101064246
                Funded by: H2020 Marie Sklodowska-Curie Actions, doi 10.13039/100010665;
                Award ID: 841466
                Categories
                Letter
                Custom metadata
                nl1c04830
                nl1c04830

                Nanotechnology
                protein sizing,nanofluidics,single molecules,confocal detection,microfluidics,biosensing

                Comments

                Comment on this article