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Solid‐State Nanopore Detection of Protein Complexes: Applications in Healthcare and Protein Kinetics
Author(s) -
Freedman Kevin J.,
Bastian Arangassery R.,
Chaiken Irwin,
Kim Min Jun
Publication year - 2013
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201201423
Subject(s) - nanopore , nanotechnology , solid state , realm , protein detection , electric field , materials science , voltage , kinetics , biophysics , chemical physics , biological system , chemistry , computer science , physics , biology , engineering , electrical engineering , quantum mechanics , political science , law
Protein conjugation provides a unique look into many biological phenomena and has been used for decades for molecular recognition purposes. In this study, the use of solid‐state nanopores for the detection of gp120‐associated complexes are investigated. They exhibit monovalent and multivalent binding to anti‐gp120 antibody monomer and dimers. In order to investigate the feasibility of many practical applications related to nanopores, detection of specific protein complexes is attempted within a heterogeneous protein sample, and the role of voltage on complexed proteins is researched. It is found that the electric field within the pore can result in unbinding of a freely translocating protein complex within the transient event durations measured experimentally. The strong dependence of the unbinding time with voltage can be used to improve the detection capability of the nanopore system by adding an additional level of specificity that can be probed. These data provide a strong framework for future protein‐specific detection schemes, which are shown to be feasible in the realm of a ‘real‐world’ sample and an automated multidimensional method of detecting events.

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