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      Atomic force microscopy-based characterization and design of biointerfaces

      , , , , ,
      Nature Reviews Materials
      Springer Nature

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          Atomic Force Microscope

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            Reversible unfolding of individual titin immunoglobulin domains by AFM.

            Single-molecule atomic force microscopy (AFM) was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. At large extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobulin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.
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              Translating biomolecular recognition into nanomechanics.

              We report the specific transduction, via surface stress changes, of DNA hybridization and receptor-ligand binding into a direct nanomechanical response of microfabricated cantilevers. Cantilevers in an array were functionalized with a selection of biomolecules. The differential deflection of the cantilevers was found to provide a true molecular recognition signal despite large nonspecific responses of individual cantilevers. Hybridization of complementary oligonucleotides shows that a single base mismatch between two 12-mer oligonucleotides is clearly detectable. Similar experiments on protein A-immunoglobulin interactions demonstrate the wide-ranging applicability of nanomechanical transduction to detect biomolecular recognition.
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                Author and article information

                Journal
                Nature Reviews Materials
                Nat. Rev. Mater.
                Springer Nature
                2058-8437
                March 14 2017
                March 14 2017
                : 2
                : 5
                : 17008
                Article
                10.1038/natrevmats.2017.8
                0f1ca05c-5d30-4dcc-b22c-5c19fe2a8aff
                © 2017
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