Skip to main content Accessibility help
×
Hostname: page-component-848d4c4894-wzw2p Total loading time: 0 Render date: 2024-04-30T13:35:21.950Z Has data issue: false hasContentIssue false

7 - Nanoscale biomemory device composed of recombinant protein variants

from Part I - Electronic components

Published online by Cambridge University Press:  05 September 2015

Ajay Kumar Yagati
Affiliation:
Sogang University
Junhong Min
Affiliation:
Chung-Ang University
Jeong Woo Choi
Affiliation:
Sogang University
Sandro Carrara
Affiliation:
École Polytechnique Fédérale de Lausanne
Krzysztof Iniewski
Affiliation:
Redlen Technologies Inc., Canada
Get access

Summary

Abstract

Recent research in nanobioelectronic devices has opened up a new wave of enthusiasm in revolutionizing electronic circuit design, marking the beginning of a new era for biomimicry phenomena to advance into high-density logic and memory applications. This chapter describes the formation and development of a protein-based biomemory device composed of recombinant protein variants, together with some experimental results on protein film formation with various readout mechanisms for constructing future memory devices. To elucidate the concept of the memory device, a redox protein in which cysteine residues were incorporated by recombinant technology was immobilized on a gold electrode surface. Application of the correct potentials then causes carrier trapping or detrapping in protein films to occur, as shown by the electrochemical measurements, thus performing the memory function. The chapter also summarizes recent research on nanoscale biomemory devices, considering first the basic nature of the write-once-read-many (WORM) characteristics. The concept of WORM is then extended to multi-bit storage of protein variants and towards development of a nanoscale biomemory device. The fact that these developed devices, operating at very low voltages, can be patterned and addressed locally, and also have good stability with excellent reversibility, makes them a promising platform for non-volatile memory devices.

Type
Chapter
Information
Handbook of Bioelectronics
Directly Interfacing Electronics and Biological Systems
, pp. 86 - 102
Publisher: Cambridge University Press
Print publication year: 2015

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Leong, M., Doris, B., Kedzierski, J., Rim, K. and Yang, M.. “Silicon device scaling to the sub-10-nm regime,” Science, Vol. 306, pp. 2057–2060, Dec. 2004.Google Scholar
Rueckes, T., Kim, K., Joselevich, E. et al. “Carbon nanotube-based nonvolatile random access memory for molecular computing,” Science, Vol. 289, pp. 94–97, Jul. 2000.CrossRefGoogle ScholarPubMed
Yin, P., Choi, H. M. T., Calvert, C. R. and Pierce, N. A.. “Programming biomolecular self-assembly pathways,” Nature, Vol. 451, pp 318–323, Jan 2008.CrossRefGoogle ScholarPubMed
Benenson, Y., Paz-Elizur, T., Adar, R. et al. “Programmable and autonomous computing machine made of biomolecules,” Nature, Vol. 414, pp 430–434, Nov 2001.CrossRefGoogle ScholarPubMed
Chua, J. H., Chee, R.-E., Agarwal, A., Wong, S. M. and Zhang, G.-J.. “Label-free electrical detection of cardiac biomarker with complementary metal-oxide semiconductor-compatible silicon nanowire sensor arrays,” Anal. Chem., Vol. 81, pp 6266–6271, July 2009.CrossRefGoogle ScholarPubMed
Rinaldi, R., Biasco, A., Maruccio, G. et al. “Electronic rectification in protein devices,” Appl. Phys. Lett., Vol. 82, pp 472, Oct. 2003.CrossRefGoogle Scholar
Xu, D., Watt, G. D., Harb, J. N. and Davis, R. C.. “Electrical conductivity of ferritin proteins by conductive AFM,” Nano Lett., Vol. 5, pp 571–577, Mar. 2005.CrossRefGoogle ScholarPubMed
Chen, Y.-S., Hong, M.-Y. and Huang, G. S.. “A protein transistor made of an antibody molecule and two gold nanoparticles,” Nature Nanotech. Vol. 7, pp 197–203, Feb. 2012.CrossRefGoogle ScholarPubMed
D´Amico, S., Maruccio, G., Visconti, P. et al. “Ambipolar transistors based on azurin proteins,” IEE Proc.-Nanobiotechnol., Vol. 151, pp 173–175, Oct. 2005.CrossRefGoogle Scholar
Mentovich, E. D., Belgorodsky, B., Kalifa, I., Cohen, H. and Richter, S.. “Large-scale fabrication of 4-nm-channel vertical protein-based ambipolar transistors,” Nano Lett., Vol. 9, pp. 1296–1300, Jan. 2009.CrossRefGoogle ScholarPubMed
Saghatelian, A., Volcker, N. H., Guckian, K. M., Lin, V. S.-Y. and Ghadiri, M. R.. “DNA-based photonic logic gates: AND, NAND, and INHIBIT,” J. Am. Chem. Soc., Vol. 125, pp. 346–347, Dec. 2002.CrossRefGoogle Scholar
Kim, S.-U., Yagati, A. K., Singh, R. P., Min, J. and Choi, J.-W.. “Charge storage investigation in self-assembled monolayer of redox-active recombinant azurin,” Curr. Appl. Phys., Vol. 9, pp. e71–e75, Mar. 2009.CrossRefGoogle Scholar
Kim, S.-U., Yagati, A.K., Min, J. and Choi, J.-W.. “Biomemory device composed of mutant azurin thin films modified by site-directed mutagenesis,” Thin Solid Films, Vol. 518, pp. 682–687, Nov. 2009.CrossRefGoogle Scholar
Pia, E. A. D., Chi, Q., Macdonald, J. E. et al. “Fast electron transfer through a single molecule natively structured redox proteinNanoscale, Vol. 4, pp. 7106–7113, Sep. 2012.Google ScholarPubMed
Choi, M., Shin, S. and Davidson, V. L.. “Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex,” Biochemistry, Vol. 51, pp. 6942–6949, Aug. 2012.CrossRefGoogle ScholarPubMed
Ventra, M. D., Pershin, Y. V.. “Biologically-inspired electronics with memory circuit elements” in Advances in Neuromorphic Memristor Science and Applications, Vol. 4. Springer Series in Cognitive and Neural Systems, 2012, pp. 15–36.CrossRefGoogle Scholar
Yagati, A. K., Kim, S.-U., Min, J. and Choi, J.-W.. “Ferredoxin molecular thin film with intrinsic switching mechanism for biomemory application,” J. Nanosci. Nanotechnol., Vol. 10, pp. 3220–3223, May 2010.CrossRefGoogle ScholarPubMed
Kim, S.-U., Lee, T., Lee, J.-H., et al.“Nanoscale film formation of ferritin and its application to biomemory device,” Ultramicroscopy, Vol. 109, pp. 974–979, July 2009.CrossRefGoogle ScholarPubMed
Cancino, J., Machado, S. A. S.. “Microelectrode array in mixed alkanethiol self-assembled monolayers: Electrochemical studies,” Electrochimica Acta, Vol. 72, pp. 108–113, June 2012.CrossRefGoogle Scholar
Rossi, E. A., Goldenberg, D. M. and Chang, C.-H., “The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures,” Bioconjugate Chem., Vol. 23, pp 309–323, Dec. 2012.CrossRefGoogle ScholarPubMed
Yagati, A. K., Kim, S.-U., Min, J. and Choi, J.-W.. “Write-Once–Read-Many-Times (WORM) biomemory device consisting of cysteine modified ferredoxin,” Electrochem. Commun., Vol. 11, pp 854–858, April 2009.CrossRefGoogle Scholar
Yagati, A. K., Kim, S.-U., Min, J. and Choi, J.-W.. “Multi-bit biomemory consisting of recombinant protein variants, azurin,” Biosens. Bioelectron., Vol. 24, pp. 1503–1507, Jan. 2009.CrossRefGoogle ScholarPubMed
Lee, T., Kim, S.-U., Min, J. and Choi, J.-W.. “Multilevel biomemory device consisting of recombinant azurin/cytochrome c,” Adv. Mater., Vol. 22, pp. 510–514, 2010.CrossRefGoogle ScholarPubMed
Lee, T., Min, J., Kim, S.-U., and Choi, J.-W.. “Multifunctional 4-bit biomemory chip consisting of recombinant azurin variants,” Biomaterials, Vol. 32, pp. 3815–3821, May 2011.CrossRefGoogle ScholarPubMed
Kim, K.-H., Gaba, S., Wheeler, D., et al. “A functional hybrid memristor crossbar-array/CMOS system for data storage and neuromorphic applications,” Nano Lett., Vol. 12, pp. 389–395, Dec. 2012.CrossRefGoogle ScholarPubMed
Park, W. I., Yoon, J. M., Park, M. et al. “Self-assembly-induced formation of high-density silicon oxide memristor nanostructures on graphene and metal electrodes,” Nano Lett., Vol. 12, pp. 1235–1240, Feb. 2012.CrossRefGoogle ScholarPubMed
Yang, Y., Sheridan, P. and Lu, W.. “Complementary resistive switching in tantalum oxide-based resistive memory devices,” Appl. Phys. Lett., Vol. 100, pp. 203112 (4pp), May 2012.CrossRefGoogle Scholar
Xie, Z., Zhou, X., Tao, X. and Zheng, Z.. “Polymer nanostructures made by scanning probe lithography: Recent progress in material applications,” Macromol. Rapid Commun., Vol. 33, pp. 359–373, Mar. 2012.CrossRefGoogle ScholarPubMed
Almawlawi, D., Bosnick, K. A., Osika, A. and Moskovits, M.. “Fabrication of nanometer-scale patterns by ion-milling with porous anodic alumina masks,” Adv. Mater., Vol. 12, pp. 1252–1257, Sep. 2000.3.0.CO;2-0>CrossRefGoogle Scholar
Wang, L., Solak, H. H. and Ekinci, Y.. “Fabrication of high-resolution large-area patterns using EUV interference lithography in a scan-exposure mode,” Nanotechnology, Vol. 23, pp. 305303 (5pp), July 2012.CrossRefGoogle Scholar
Deng, X., Ma, Y., Zhang, P. et al.“Investigation of shadow effect in laser-focused atomic deposition,” Appl. Surf. Sci., Vol. 261, pp. 464–469, Nov. 2012.CrossRefGoogle Scholar
Röder, H., Hahn, E., Brune, H., Bucher, J.-P. and Kern, K.. “Building one- and two-dimensional nanostructures by diffusion-controlled aggregation at surfaces,” Nature, Vol. 366, pp. 141–143, Nov. 1993.CrossRefGoogle Scholar
Kleineberg, U., Brechling, A., Sundermann, M. and Heinzmann, U.. “STM lithography in an organic self-assembled monolayer,” Adv. Funct. Mater., Vol. 11, pp. 208–212, June 2001.3.0.CO;2-X>CrossRefGoogle Scholar
Hurley, C. R., Ducker, R. E., Leggett, G. J. and Ratner, B. D.. “Fabrication of submicrometer biomolecular patterns by near-field exposure of plasma-polymerized tetraglyme films,” Langmuir, Vol. 26, pp. 10203–10209, Mar. 2010.CrossRefGoogle ScholarPubMed
Sun, J., Zhang, H., Tian, R. et al. “Ultrafast enzyme immobilization over large-pore nanoscale mesoporous silica particles,” Chem. Commun., Issue 12, pp. 1322–1324, Feb. 2006.CrossRefGoogle ScholarPubMed
Martin, T. A., Caliari, S. R., Williford, P. D., Harley, B. A. and Bailey, R. C.. “The generation of biomolecular patterns in highly porous collagen-GAG scaffolds using direct photolithography,” Biomaterials, Vol. 32, pp. 3949–3957, Jun. 2011.CrossRefGoogle ScholarPubMed
Whitney, A. V., Myers, B. D. and Van Duyne, R. P.. “Sub-100 nm triangular nanopores fabricated with the reactive ion etching variant of nanosphere lithography and angle-resolved nanosphere lithography,” Nano Lett., Vol. 4, pp. 1507–1511, June 2004.CrossRefGoogle Scholar
Yagati, A. K., Jung, M., Kim, S.-U., Min, J. and Choi, J.-W.. “Nanoscaled redox active protein adsorption on Au-dot arrays: An electrochemical scanning probe microscopic investigation for application in nano-biodevices,” Thin Solid Films, Vol. 518, pp. 634–637, Nov. 2009.CrossRefGoogle Scholar
Hansen, A. G., Salvatore, P., Karlsen, K. K. et al. “Electrochemistry and in situ scanning tunnelling microscopy of pure and redox-marked DNA- and UNA-based oligonucleotides on Au(111)-electrode surfaces,” Phys. Chem. Chem. Phys., Vol. 15, pp. 776–786, May 2013.CrossRefGoogle ScholarPubMed
Kim, S.-U., Yagati, A. K., Min, J. and Choi, J.-W.. “Nanoscale protein-based memory device composed of recombinant azurin,” Biomaterials, Vol. 31, pp 1293–1298, Feb. 2010.CrossRefGoogle ScholarPubMed
Yagati, A.K., Lee, T., Min, J. and Choi, J.-W.. “A robust nanoscale biomemory device composed of recombinant azurin on hexagonally packed Au-nano array,” Biosens. Bioelectron., Vol. 40, pp. 283–290, Feb. 2013.CrossRefGoogle ScholarPubMed
Soloman, E. I., Hare, J.W., Dooley, D.M. et al. “Spectroscopic studies of stellacyanin, plastocyanin, and azurin. Electronic structure of the blue copper sites,” J. Am. Chem. Soc., Vol. 102, pp. 168–178, Jan. 1980.CrossRefGoogle Scholar
Han, J., Loehr, T. M., Li, Y. et al. “Resonance raman excitation profiles indicate multiple Cys→Cu charge transfer transitions in type 1 copper proteins,” J. Am. Chem. Soc., Vol. 115, pp. 4256–4263, May 1993.CrossRefGoogle Scholar
Groeneveld, C. M. and Canters, G. W.. “The pH dependence of the electron self-exchange rate of azurin from Pseudomonas aeruginosa as studied by 1H-NMR,” Eur. J. Biochem., Vol. 153, pp. 559–564, Dec.1985.CrossRefGoogle Scholar

Save book to Kindle

To save this book to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×