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Nano Biomedicine and Engineering 2023, 15(2): 96-104 https://doi.org/10.26599/NBE.2023.9290009
Research Article | Open Access | Issue | Published: 09 May 2023

Immobilization of Thai Population-specific Human Leukocyte Antigens on Magnetic Nanoparticles Integrated with Nuclear Magnetic Resonance Technology

Show Author's Information Wichai Subtaweewasin( ),  Wanchai Pijitrojana( )
Department of Electrical and Computer Engineering, Thammasat School of Engineering, Thammasat University, Pathumthani, Thailand
Keywords:
magnetic nanoparticles, immobilization, human leukocyte antigen, micro-nuclear magnetic resonance, human leukocyte antigens antibody, kidney transplantation
Cite this article:
Subtaweewasin W, Pijitrojana W. Immobilization of Thai Population-specific Human Leukocyte Antigens on Magnetic Nanoparticles Integrated with Nuclear Magnetic Resonance Technology. Nano Biomedicine and Engineering, 2023, 15(2): 96-104. https://doi.org/10.26599/NBE.2023.9290009
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Abstract Full text About this article

Kidney disease, as a global health problem, can progress to kidney failure. Kidney transplantation is a treatment option for end-stage disease and an alternative to dialysis. Complement-dependent cytotoxicity tests and flow cytometry are methods used to test for compatibility between autoantibodies and donor recipient. Antibodies against donor human leukocyte antigens (HLAs), linked to hyperacute or severely acute rejection, frequently result in graft loss. Currently, fluorescent bead assay (Luminex®) technology is used in Thailand for HLA–antibody typing tests. However, each test requires specific location and time, expensive equipment, and high costs. The goal of such research is that, HLA–antibody typing tests can be performed wherever it is the most convenient for recipients and hospitals. A further advantage is that the surgeon can perform a final test for confirmation before the surgery. Numerous technologies are currently available for this purpose. The focus of this study was on the Fe3O4 magnetic nanoparticles (MNPs) immobilized with HLAs frequently found in the Thai population. These were examined using nuclear magnetic resonance (NMR) to measure HLA antibody typing. MNPs have recently attracted considerable attention because of their strong magnetization and large surface areas. Immobilization reactions with antigens and the straightforward magnetic separation of MNPs are low-cost techniques. Hence, the commercialization of Fe3O4 MNPs is favorable. In this study, MNPs were functionalized with 3-aminopropyl triethoxysilane (APTES) in toluene and ethanol, and the nanoparticles were streptavidin activated after APTES treatment. A specific biotinylated HLA for the Thai population was used and immobilized on streptavidin. The MNPs were effectively immobilized. The magnetic properties can be modified by adding other ions to Fe3O4. We discovered that the shape and size variations of Fe3O4 MNPs may have an impact on the amount of functionalized and immobilized surface area.


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About this article

Immobilization of Thai Population-specific Human Leukocyte Antigens on Magnetic Nanoparticles Integrated with Nuclear Magnetic Resonance Technology

Show Author's information Wichai Subtaweewasin( ), Wanchai Pijitrojana( )
Department of Electrical and Computer Engineering, Thammasat School of Engineering, Thammasat University, Pathumthani, Thailand

Abstract

Kidney disease, as a global health problem, can progress to kidney failure. Kidney transplantation is a treatment option for end-stage disease and an alternative to dialysis. Complement-dependent cytotoxicity tests and flow cytometry are methods used to test for compatibility between autoantibodies and donor recipient. Antibodies against donor human leukocyte antigens (HLAs), linked to hyperacute or severely acute rejection, frequently result in graft loss. Currently, fluorescent bead assay (Luminex®) technology is used in Thailand for HLA–antibody typing tests. However, each test requires specific location and time, expensive equipment, and high costs. The goal of such research is that, HLA–antibody typing tests can be performed wherever it is the most convenient for recipients and hospitals. A further advantage is that the surgeon can perform a final test for confirmation before the surgery. Numerous technologies are currently available for this purpose. The focus of this study was on the Fe3O4 magnetic nanoparticles (MNPs) immobilized with HLAs frequently found in the Thai population. These were examined using nuclear magnetic resonance (NMR) to measure HLA antibody typing. MNPs have recently attracted considerable attention because of their strong magnetization and large surface areas. Immobilization reactions with antigens and the straightforward magnetic separation of MNPs are low-cost techniques. Hence, the commercialization of Fe3O4 MNPs is favorable. In this study, MNPs were functionalized with 3-aminopropyl triethoxysilane (APTES) in toluene and ethanol, and the nanoparticles were streptavidin activated after APTES treatment. A specific biotinylated HLA for the Thai population was used and immobilized on streptavidin. The MNPs were effectively immobilized. The magnetic properties can be modified by adding other ions to Fe3O4. We discovered that the shape and size variations of Fe3O4 MNPs may have an impact on the amount of functionalized and immobilized surface area.

Keywords: magnetic nanoparticles, immobilization, human leukocyte antigen, micro-nuclear magnetic resonance, human leukocyte antigens antibody, kidney transplantation

References(49)

[1]

N. Larpparisuth, W. Cheungpasitporn, A. Lumpaopong. Global perspective on kidney transplantation: Thailand. Kidney360, 2021, 2(7): 1163−1165. https://doi.org/10.34067/KID.0002102021
DOI Google Scholar
[2]
P. Rianthavorn. 2019 Annual Report of Organ Transplantation in Thailand. Thai Transplantation Society, 2019.
[3]

P. Kupatawintu, S. Pheancharoen, A. Srisuddee, et al. HLA-A, -B, -DR haplotype frequencies in the Thai stem cell donor registry. Tissue Antigens, 2010, 75(6): 730−736. https://doi.org/10.1111/j.1399-0039.2010.01450.x
DOI Google Scholar
[4]
S. Ounjai, P. P., S. Kanunthong, A. Srisuddee, et al. HLA-A, -B, and -DR frequencies in deceased kidney donors from the Organ Donation Center Thai Red Cross Society. Journal of Hematology and Transfusion Medicine, 2019, 29: 175–181. (in Thai)
[5]

B.H. Chung, Y.Y. Joo, J. Lee, et al. Impact of ABO incompatibility on the development of acute antibody-mediated rejection in kidney transplant recipients presensitized to HLA. PLoS One, 2015, 10(4): e0123638. https://doi.org/10.1371/journal.pone.0123638
DOI Google Scholar
[6]

B. Clark, D.J. Unsworth. HLA and kidney transplantation. Journal of Clinical Pathology, 2010, 63(1): 21−25. https://doi.org/10.1136/jcp.2009.072785
DOI Google Scholar
[7]

E. Lougee, S. Morjaria, O. Shaw, et al. A new approach to HLA typing designed for solid organ transplantation: Epityping and its application to the HLA-a locus. International Journal of Immunogenetics, 2013, 40(6): 445−452. https://doi.org/10.1111/iji.12053
DOI Google Scholar
[8]

B.D. Tait. Detection of HLA antibodies in organ transplant recipients-triumphs and challenges of the solid phase bead assay. Frontiers in Immunology, 2016, 7: 570. https://doi.org/10.3389/fimmu.2016.00570
DOI Google Scholar
[9]

G. Wang, C. Wang, R. Yang, et al. A sensitive and stable surface plasmon resonance sensor based on monolayer protected silver film. Sensors, 2017, 17(12): E2777. https://doi.org/10.3390/s17122777
DOI Google Scholar
[10]

J.T. Liu, P.S. Lin, Y.M. Hsin, et al. Surface plasmon resonance biosensor for microalbumin detection. Journal of the Taiwan Institute of Chemical Engineers, 2011, 42(5): 696−700. https://doi.org/10.1016/j.jtice.2011.01.005
DOI Google Scholar
[11]

H. Ahn, H. Song, J.R. Choi, et al. A localized surface plasmon resonance sensor using double-metal-complex nanostructures and a review of recent approaches. Sensors, 2017, 18(1): E98. https://doi.org/10.3390/s18010098
DOI Google Scholar
[12]

N. Kostevšek. A review on the optimal design of magnetic nanoparticle-based T2 MRI contrast agents. Magnetochemistry, 2020, 6(1): 11. https://doi.org/10.3390/magnetochemistry6010011
DOI Google Scholar
[13]

O.V. Shynkarenko, S.A. Kravchenko. Surface plasmon resonance sensors: Methods of surface functionalization and sensitivity enhancement. Theoretical and Experimental Chemistry, 2015(5): 273. https://doi.org/10.1007/s11237-015-9427-5
DOI Google Scholar
[14]

L.A. Lyon, M.D. Musick, M.J. Natan. Colloidal Au-enhanced surface plasmon resonance immunosensing. Analytical Chemistry, 1998, 70(24): 5177−5183. https://doi.org/10.1021/ac9809940
DOI Google Scholar
[15]
A. Dupré, K.M. Lei, P.I. Mak, et al. Micro- and nanofabrication NMR technologies for point-of-care medical applications–A review. Microelectronic Engineering, 2019. 209: 66–74.
DOI
[16]
Y. Liu, N. Sun, H. Lee, et al. CMOS mini nuclear magnetic resonance system and its application for biomolecular sensing. In: Proceedings of 2008 IEEE International Solid-State Circuits Conference, 2008.
DOI
[17]

Y. Sahoo, A. Goodarzi, M.T. Swihart, et al. Aqueous ferrofluid of magnetite nanoparticles:   fluorescence labeling and magnetophoretic control. The Journal of Physical Chemistry B, 2005, 109(9): 3879−3885. https://doi.org/10.1021/jp045402y
DOI Google Scholar
[18]

Y. Mizukoshi, S. Seino, K. Okitsu, et al. Sonochemical preparation of composite nanoparticles of Au/gamma-Fe2O3 and magnetic separation of glutathione. Ultrasonics Sonochemistry, 2005, 12(3): 191−195. https://doi.org/10.1016/j.ultsonch.2003.12.003
DOI Google Scholar
[19]

V.M. Costa, M.C.M. de Souza, P.B.A. Fechine, et al. Nanobiocatalytic systems based on lipase-Fe3O4 and conventional systems for isoniazid synthesis: A comparative study. Brazilian Journal of Chemical Engineering, 2006, 33: 661−673. https://doi.org/10.1590/0104-6632.20160333s20150137
DOI Google Scholar
[20]

J.K. Xu, J.J. Sun, Y.J. Wang, et al. Application of iron magnetic nanoparticles in protein immobilization. Molecules, 2014, 19(8): 11465−11486. https://doi.org/10.3390/molecules190811465
DOI Google Scholar
[21]

J.C. Gorga, A. Dong, M.C. Manning, et al. Comparison of the secondary structures of human class I and class II majors histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy. Proceedings of the National Academy of Sciences, 1989, 86(7): 2321−2325. https://doi.org/10.1073/pnas.86.7.2321
DOI Google Scholar
[22]

N. Gunawansa, R. Rathore, A. Sharma, et al. Crossmatch strategies in renal transplantation: A practice guide for the practicing clinician. Journal of Transplant Surgery, 2017, 1(1): 8−15. https://doi.org/10.36959/338/325
DOI Google Scholar
[23]

S. Ferrari-Lacraz, J.M. Tiercy, J. Villard. Detection of anti-HLA antibodies by solid-phase assay in kidney transplantation: Friend or foe. Tissue Antigens, 2012, 79(5): 315−325. https://doi.org/10.1111/j.1399-0039.2012.01853.x
DOI Google Scholar
[24]

H.Y. Song, J. Hobley, X. Su, et al. End-on covalent antibody immobilization on dual polarization interferometry sensor chip for enhanced immuno-sensing. Plasmonics, 2014, 9(4): 851−858. https://doi.org/10.1007/s11468-014-9680-9
DOI Google Scholar
[25]

N.K. Mehra, A.K. Baranwal. Clinical and immunological relevance of antibodies in solid organ transplantation. International Journal of Immunogenetics, 2016, 43(6): 351−368. https://doi.org/10.1111/iji.12294
DOI Google Scholar
[26]

R.J. Duquesnoy, M. Marrari. Correlations between terasaki’s HLA class I epitopes and HLAMatchmaker-defined eplets on HLA-A, -B and-C antigens. Tissue Antigens, 2009, 74(2): 117−133. https://doi.org/10.1111/j.1399-0039.2009.01271.x
DOI Google Scholar
[27]

J.M. Greene, R.W. Wiseman, S.M. Lank, et al. Differential MHC class I expression in distinct leukocyte subsets. BMC Immunology, 2011, 12: 39. https://doi.org/10.1186/1471-2172-12-39
DOI Google Scholar
[28]

P. Molek, T. Bratkovič. Epitope mapping of mono- and polyclonal antibodies by screening phage-displayed random peptide libraries. Acta Chimica Slovenica, 2016, 63(4): 914−919. https://doi.org/10.17344/acsi.2016.2458
DOI Google Scholar
[29]

A. Man-Kupisinska, M. Michalski, A. Maciejewska, et al. A new ligand-based method for purifying active human plasma-derived ficolin-3 complexes supports the phenomenon of crosstalk between pattern-recognition molecules and immunoglobulins. PLoS One, 2016, 11(5): e0156691. https://doi.org/10.1371/journal.pone.0156691
DOI Google Scholar
[30]
C.S.M. Kramer, D.L. Roelen, S. Heidt, et al. Defining the immunogenicity and antigenicity of HLA epitopes is crucial for optimal epitope matching in clinical renal transplantation. HLA, 2017, 90(1): 5–16.
DOI
[31]

N. Sun, Y. Liu, H. Lee, et al. CMOS RF biosensor utilizing nuclear magnetic resonance. IEEE Journal of Solid-State Circuits, 2009, 44(5): 1629−1643. https://doi.org/10.1109/jssc.2009.2017007
DOI Google Scholar
[32]
M. Ylmaz, C. Ozic, I. Gok. Principles of nucleic acid separation by agarose gel electrophoresis. In: Gel Electrophoresis—Principles and Basics, 2012.
DOI
[33]

K.M. Lei, P.I. Mak, M.K. Law, et al. A palm-size μNMR relaxometer using a digital microfluidic device and a semiconductor transceiver for chemical/biological diagnosis. The Analyst, 2015, 140(15): 5129−5137. https://doi.org/10.1039/c5an00500k
DOI Google Scholar
[34]

Y.L. Luo, E.C. Alocilja. Portable nuclear magnetic resonance biosensor and assay for a highly sensitive and rapid detection of foodborne bacteria in complex matrices. Journal of Biological Engineering, 2017, 11: 14. https://doi.org/10.1186/s13036-017-0053-8
DOI Google Scholar
[35]

S. Sabban, H.T. Ye, B. Helm. Development of an in vitro model system for studying the interaction of Equus caballus IgE with its hight-affinity FcεRI receptor. Jounrnal of Visualized Experiments, 2014, 93: e52222. https://doi.org/10.3791/52222
DOI Google Scholar
[36]

A.K. Gupta, R.R. Naregalkar, V.D. Vaidya, et al. Recent advances on surface engineering of magnetic iron oxide nanoparticles and their biomedical applications. Nanomedicine, 2007, 2(1): 23−39. https://doi.org/10.2217/17435889.2.1.23
DOI Google Scholar
[37]

K.S. Park, H. Kim, S. Kim, et al. Nanomagnetic system for rapid diagnosis of acute infection. ACS Nano, 2017, 11(11): 11425−11432. https://doi.org/10.1021/acsnano.7b06074
DOI Google Scholar
[38]

H.Y. Lin, C.H. Huang, J. Park, et al. Integrated magneto-chemical sensor for on-site food allergen detection. ACS Nano, 2017, 11(10): 10062−10069. https://doi.org/10.1021/acsnano.7b04318
DOI Google Scholar
[39]

A.C. Barreto, F.J.N. Maia, V.R. Santiago, et al. Novel ferrofluids coated a renewable material obtained from cashew nut shell liquid. Microfluidics and Nanofluidics, 2011, 12(5): 677−686. https://doi.org/10.1007/s10404-011-0910-6
DOI Google Scholar
[40]

Can, K., Ozmen, M., Ersoz, M. Immobilization of albumin on aminosilane modified superparamagnetic magnetite nanoparticles and its characterization. Colloids and Surfaces B,Biointerfaces, 2009, 71(1): 154−159. https://doi.org/10.1016/j.colsurfb.2009.01.021
DOI Google Scholar
[41]

J.S. Choi, S. Kim, D. Yoo, et al. Distance-dependent magnetic resonance tuning as a versatile MRI sensing platform for biological targets. Nature Materials, 2017, 16(5): 537−542. https://doi.org/10.1038/NMAT4846
DOI Google Scholar
[42]

J.T. Jang, H. Nah, J.H. Lee, et al. Critical enhancements of MRI contrast and hyperthermic effects by dopant-controlled magnetic nanoparticles. Angewandte Chemie, 2009, 48(7): 1234−1238. https://doi.org/10.1002/ange.200805149
DOI Google Scholar
[43]

A. Cavalli, X. Salvatella, C.M. Dobson, et al. Protein structure determination from NMR chemical shifts. Proceedings of the National Academy of Sciences of the United States of America, 2007, 104(23): 9615−9620. https://doi.org/10.1073/pnas.0610313104
DOI Google Scholar
[44]

R. Li, F. Feng, Z.Z. Chen, et al. Sensitive detection of carcinoembryonic antigen using surface plasmon resonance biosensor with gold nanoparticles signal amplification. Talanta, 2015, 140: 143−149. https://doi.org/10.1016/j.talanta.2015.03.041
DOI Google Scholar
[45]

W.A. Talavera-Pech, A. Esparza-Ruiz, P. Quintana-Owen, et al. Effects of different amounts of APTES on physicochemical and structural properties of amino-functionalized MCM-41- MSNs. Journal of Sol-Gel Science and Technology, 2016, 80(3): 697−708. https://doi.org/10.1007/s10971-016-4163-4
DOI Google Scholar
[46]

S. Sajjadifar, Z. Gheisarzadeh. Isatin-SO3H coated on amino propyl modified magnetic nanoparticles (Fe3O4@APTES@isatin-SO3H) as a recyclable magnetic nanoparticle for the simple and rapid synthesis of pyrano[2,3-d] pyrimidines derivatives. Applied Organometallic Chemistry, 2018, 33(1): e4602. https://doi.org/10.1002/aoc.4602
DOI Google Scholar
[47]

B.T. Thanh, N. Van Sau, H. Ju, et al. Immobilization of protein A on monodisperse magnetic nanoparticles for biomedical applications. Journal of Nanomaterials, 2019, 2019: 1−9. https://doi.org/10.1155/2019/2182471
DOI Google Scholar
[48]

B. Thangaraj, Z. Jia, L. Dai, et al. Effect of silica coating on Fe3O4 magnetic nanoparticles for lipase immobilization and their application for biodiesel production. Arabian Journal of Chemistry, 2016, 12(8): 4694−4706. https://doi.org/10.1016/j.arabjc.2016.09.004
DOI Google Scholar
[49]

S.F. Chew, B.R. Wood, C. Kanaan, et al. Fourier transform infrared imaging as a method for detection of HLA class I expression in melanoma without the use of antibody. Tissue Antigens, 2007, 69(Suppl 1): 252−258. https://doi.org/10.1111/j.1399-0039.2006.00775.x
DOI Google Scholar
Publication history
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Publication history

Received: 30 December 2022
Revised: 06 March 2023
Accepted: 27 March 2023
Published: 09 May 2023
Issue date: June 2023

Copyright

© The Author(s) 2023.

Acknowledgements

Acknowledgement

The author would like to thank this research and innovation activity is funded by National Research Council of Thailand (NRCT) and Thammasat School of Engineering for the research grant to conduct the research, and Thammasat School of Engineering, Thammasat University for the scholarship.

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