Skip to main content
. Author manuscript; available in PMC: 2021 Jun 1.
Published in final edited form as: Anal Bioanal Chem. 2020 Apr 21;412(16):3801–3811. doi: 10.1007/s00216-020-02623-7

Figure 2.

Figure 2.

Seminal dielectrophoretic collections of proteins. A) Original DEP trapping data for protein (fluorescently labeled avidin) using interdigitated sinusoidally corrugated electrodes (Figure 1D). Proteins (avidin and chymotripsinogen) were shown to be reversibly collected (© 1994 by the Institute of Electrical and Electronics Engineers, reproduced with permission).[7] B) Using a nanopipette tip as a gradient inducing structure, labeled protein G is captured exactly at the tip of the entrance (white spot in sub-image ‘A’ in original figure letter label). The protein is highly localized in the first micron of the pipette tip (‘E’ in original figure letter label) (© Wiley-VCH Verlag GmbH & Co. KGaA. Reproduced with permission).[19] C) Single molecule trapping at sharp nanoelectrodes using dielectrophoretic forces. R-phycoerythrin is held at the strongest gradient near the tip of electrodes spaced 0.5 μm apart (© 2005 by the American Physical Society. Reprinted figure with permission from [11]). D) Fluorescently labeled bovine serum albumin captures in an array of insulating posts at applied global potentials of (letter labeled from original cite) a: 700, b:1000, c: 1600 and d: 900 V/m (© Elsevier 2008, with permission from Elsevier, adapted from [35]).