Using Liquid Crystals to Report Membrane Proteins Captured by Affinity Microcontact Printing from Cell Lysates and Membrane Extracts

Jang, Chang‐Hyun; Tingey, Matthew L.; Korpi, N.L.; Wiepz, Gregory J.; Schiller, Joan H.; Bertics, Paul J.; Abbott, Nicholas L.

doi:10.1021/ja051079g

Cited by 72 publications

(42 citation statements)

References 17 publications

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“…The orientational properties of liquid crystals (LCs) enables the amplification and the transduction of biologically relevant binding events at nanostructured surfaces into optical outputs. [1][2][3] They can be used to image receptor-mediated binding of proteins at surfaces with submicrometer spatial resolution. 4,5 This method is potentially useful because it does not require the use of enzymatic or fluorescent labels, which largely complicate surface-based assays and prevent high levels of multiplexing.…”

Section: Introductionmentioning

confidence: 99%

Liquid Crystal-based Imaging of Biomolecular Interactions at Roller Printed Protein Surfaces

Park¹,

Jang²

2010

Bulletin of the Korean Chemical Society

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In this study, the orientational behavior of thermotropic liquid crystals (LC) supported on a film of protein receptors was examined. Avidin was roller printed and covalently immobilized onto the surface of gold using NHS/EDC chemistry. The orientation of nematic 4-cyano-4'-pentylbiphenyl (5CB) was found to be parallel to the plane of the printed avidin surface before incubation with a solution of biotin. However, protein-receptor complexation induced a random orientation of 5CB, where protein-receptor complexes disturbed the nanoscale topography of the printed protein surface. Atomic force microscopy and ellipsometry was used to confirm printing and the specific interaction of proteins. These results demonstrate that the combination of LC and roller printing can be used to detect specific interactions between biomolecules by manipulating the orientational behavior of LC to the printed protein surfaces.

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Section: Introductionmentioning

confidence: 99%

Liquid Crystal-based Imaging of Biomolecular Interactions at Roller Printed Protein Surfaces

Park¹,

Jang²

2010

Bulletin of the Korean Chemical Society

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“…[5][6][7][8][9][10][11][12][13][14] What makes LCs useful mainly stems from its optical anisotropy properties such as optical birefringence, which arises from the different refractive indices along two molecular axes of LCs, ie, n o and n e along the ordinary and the extraordinary axes, respectively. The orientations of LCs dominate changes in optical birefringence of LCs, and its control forms a basis of electro-optical switching and LC-based optical biosensors.…”

Section: Introductionmentioning

confidence: 99%

Optical birefringence of liquid crystals for label-free optical biosensing diagnosis

An¹,

Nguyen²,

Han³

et al. 2015

IJN

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Purpose We present a polarization-sensitive optical detection platform for label-free quantitative optical biosensing diagnosis using liquid crystals (LCs). This is capable of determining quantitatively the optical birefringence of optical cells containing LCs, whose orientation depends on the immobilized biomolecules. Patients and methods This technique uses a polarization-dependent double-port detection without any polarizer at a single wavelength and removes the need of aligning optical cells of LCs in the azimuthal direction, with respect to the light path through the optical cell. Thus, this technique enables a stand-alone detection in a relatively compact format without an additional optical instrument, such as a retardation compensator, a Michael–Levy chart, and a spectrophotometer, in order to determine the optical birefringence quantitatively. Results We demonstrate that bovine serum albumin immobilized on the gold surface of the cell hybrid interfaces that support both homeotropic and planar anchoring of LCs causes optical phase retardation change which can be determined quantitatively. We also provide estimation of the zenithal orientation of LCs near the gold surface of the hybrid interfaces, based on the phase retardation determined. The estimated limit of bovine serum albumin detection is approximately 2.1 μM. Conclusion This optical technique with LCs can serve an optical platform for label-free quantitative diagnosis of proteins in a real time manner.

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“…[4][5][6] One of the most important advantages of LCs-based sensors is that the orientational properties of LCs enable the sensitive amplification and transduction of a series of interactions into optical outputs that are visible to the naked eye between crossed polarizers due to the birefringence of LCs. [7][8][9] When compared with traditional analytical methods, LCs based sensors have many advantages including that they do not require labeling of substrates, complex instrumentations, or tedious sequences of actions. 4,5 Previous studies have shown that the orientational transition of LCs could be coupled to a range of biomolecular interactions such as specific-binding events and enzyme activities at planar interfaces between LCs and the aqueous phases.…”

Section: Introductionmentioning

confidence: 99%

Liquid Crystal Based Optical Sensor for Imaging Trypsin Activity at Interfaces Between Aqueous Phases and Thermotropic Liquid Crystals

Jang¹

2013

Bulletin of the Korean Chemical Society

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In this study, we developed a liquid crystal (LC)-based optical sensor for monitoring enzymatic activity through orientational changes in liquid crystals (LCs) coupled to the properties of a poly-L-lysine (PLL)-based polymeric membrane. We prepared a PLL-based polymeric membrane at the planar interface between the thermotropic liquid crystal and aqueous phases. The PLL-based polymeric membrane was obtained by contacting the PLL solution with water immiscible LCs, 4-cyano-4'-pentyl-biphenyl (5CB) doped with adipoyl chloride. We then investigated the membrane properties by examining the permeability of the membrane to phospholipids, 1,2-didodecanoyl-rac-glycero-3-phosphocholine (DLPC). The permeability of the membrane to transport phospholipids was monitored through the orientational transition of 5CB in contact with the dispersions of DLPC. Since trypsin can enzymatically catalyze the hydrolysis of PLL, we incubated an aqueous trypsin solution with the membrane for 2 h at room temperature to cause an increase in the permeability of the polymeric membrane to DLPC. As a result, a bright to dark optical shift of LCs was observed, which implied that an enzymatic reaction between trypsin and PLL-based membrane occurred. Two control experiments using chymotrypsin and bovine serum albumin (BSA) revealed no sign of improved permeability based on the orientational transition of LCs.

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Using Liquid Crystals to Report Membrane Proteins Captured by Affinity Microcontact Printing from Cell Lysates and Membrane Extracts

Cited by 72 publications

References 17 publications

Liquid Crystal-based Imaging of Biomolecular Interactions at Roller Printed Protein Surfaces

Liquid Crystal-based Imaging of Biomolecular Interactions at Roller Printed Protein Surfaces

Optical birefringence of liquid crystals for label-free optical biosensing diagnosis

Liquid Crystal Based Optical Sensor for Imaging Trypsin Activity at Interfaces Between Aqueous Phases and Thermotropic Liquid Crystals

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