Citation: Wu Chuanli, Liang Wenhui, Fan Jingjing, Cao Yuxian, Wu Ping, Cai Chenxin. Regulating Electron Transport Band Gaps of Bovine Serum Albumin by Binding Hemin[J]. Acta Physico-Chimica Sinica, ;2021, 37(3): 191205. doi: 10.3866/PKU.WHXB201912050 shu

Regulating Electron Transport Band Gaps of Bovine Serum Albumin by Binding Hemin

1.
Jiangsu Key Laboratory of New Power Batteries, Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, College of Chemistry and Materials Science, Nanjing Normal University, Nanjing 210023, China
2.
College of Education, Nanjing Normal University, Nanjing 210023, China

Corresponding author: Cai Chenxin, cxcai@njnu.edu.cn
Received Date: 23 December 2019
Revised Date: 16 January 2020
Accepted Date: 24 January 2020
Available Online: 3 March 2020
Fund Project: The project was supported by the National Natural Science Foundation of China (21335004, 21675088), the Natural Science Foundation of Jiangsu Province, China (BK20181382, BK20181383), and the Priority Academic Program Development of the Jiangsu Higher Education Institutions, Chinathe Natural Science Foundation of Jiangsu Province, China BK20181383the National Natural Science Foundation of China 21335004the National Natural Science Foundation of China 21675088the Natural Science Foundation of Jiangsu Province, China BK20181382

The small size (nanoscale) of proteins and their favorable electron transport (ETp) properties make them suitable for various types of bioelectronic devices and offer a solution for miniaturizing these devices to nanoscale dimensions. The performance of protein-based devices is predominantly affected by the ETp property of the proteins, which is largely determined by the band gaps of the proteins, i.e., the energy difference between the conduction band (CB) and valence band (VB). Regulating the protein ETp band gaps to appropriate values is experimentally demanding and hence remains a significant challenge. This study reports a facile method for modulating the ETp band gaps of bovine serum albumin (BSA), via its binding with a foreign molecule, hemin. The formation of the hemin-BSA complex was initially confirmed by theoretical simulation (molecular docking) and experimental characterization (fluorescence and absorption spectra), which indicated that the hemin is positioned inside a hydrophobic cavity formed by hydrophobic amino acid residues and near Trp213, at subdomain IIA of BSA, with no significant effects on the structure of BSA. Circular dichroism (CD) spectra indicated that the BSA conformation remains essentially unaltered following the formation of the hemin-BSA complex, as the helicities of the free BSA (non-binding) and the hemin-BSA complex were estimated to be 66% and 65%, respectively. Moreover, this structural conformation remains preserved after the hemin-BSA complex is immobilized on the Au substrate surface. The hemin-BSA complex is immobilized onto the Au substrate surface along a single orientation, via the ―SH group of Cys34 on the protein surface. Atomic force microscopy (AFM) images indicate that hemin-BSA forms a dense layer on the surface of the Au substrate with a lateral size of ~3.2‒3.7 nm, which is equivalent to the actual size of BSA, ~4.0 nm × 4.0 nm × 14.0 nm. The current-voltage (I-V) responses were measured using eutectic gallium-indium (EGaIn) as the top electrode and an Au film as the substrate electrode, revealing that the ETp processes of BSA and hemin-BSA on the Au surface have distinct semiconducting characteristics. The CB and VB were estimated by analysis of the differential conductance spectra, and for the free BSA, they were ~0.75 ± 0.04 and ~ −0.75 ± 0.08 eV, respectively, being equally distributed around the Fermi level (0 eV), with a band gap of ~1.50 ± 0.05 eV. Following hemin binding, the CB (~0.64 ± 0.06 eV) and VB (~ −0.29 ± 0.07 eV) of the protein were closer to the Fermi level, resulting in a band gap of ~0.93 ± 0.05 eV. These results demonstrated that hemin molecules can effectively regulate ETp characteristics and the transport band gap of BSA. This methodology may provide a general approach for tuning protein ETp band gaps, enabling broad variability by the preselection of binding molecules. The protein and foreign molecule complex may further serve as a suitable material for configuring nanoscale solid-state bioelectronic devices.
- Protein electron transport,
- Protein-based electronic device,
- Bovine serum albumin,
- Hemin
1. [1]
  Bostick, C. D.; Mukhopadhyay, S.; Pecht, I.; Sheves, M.; Cahen, D.; Lederman, D. Rep. Prog. Phys. 2018, 81, 026601. doi: 10.1088/1361-6633/aa85f2 doi: 10.1088/1361-6633/aa85f2
2. [2]
  Zeng, Y.; Sun, B.; Yu. H. Y.; Wang, X.; Peng H.; Chen, Y.; Zhu, S.; Mao, S. Mater. Today Chem. 2019, 13, 18e24. doi: 10.1016/j.mtchem.2019.04.008 doi: 10.1016/j.mtchem.2019.04.008
3. [3]
  Richter, S.; Mentovich, E.; Elnathan, R. Adv. Mater. 2018, 30, 1706941. doi: 10.1002/adma.201706941 doi: 10.1002/adma.201706941
4. [4]
  Fereiro, J. A.; Porat, G.; Bendikov, T.; Pecht, I.; Sheves, M.; Cahen, D. J. Am. Chem. Soc. 2018, 140, 13317. doi: 10.1021/jacs.8b07742 doi: 10.1021/jacs.8b07742
5. [5]
  Blumberger, J. Curr. Opin. Chem. Biol. 2018, 47, 24. doi: 10.1016/j.cbpa.2018.06.021 doi: 10.1016/j.cbpa.2018.06.021
6. [6]
  Amdursky, N.; Marchak, D.; Sepunaru, L.; Pecht, I.; Sheves, M.; Cahen, D. Adv. Mater. 2014, 26, 7142. doi: 10.1002/adma.201402304 doi: 10.1002/adma.201402304
7. [7]
  Ron, I.; Sepunaru, L.; Itzhakov, S.; Belenkova, T.; Friedman, N.; Pecht, I.; Sheves, M.; Cahen, D. J. Am. Chem. Soc. 2010, 132, 4131. doi: 10.1021/ja907328r doi: 10.1021/ja907328r
8. [8]
  Fereiro, J. A.; Yu, X.; Pecht, I.; Sheves, M.; Cuevas, J. C.; Cahen, D. Proc. Natl. Acad. Sci. USA 2018, 115, E4577. doi: 10.1073/pnas.1719867115 doi: 10.1073/pnas.1719867115
9. [9]
  Metkar, S. K.; Girigoswami, K. Biocatal. Agric. Biotechnol. 2019, 17, 271. doi: 10.1016/j.bcab.2018.11.029 doi: 10.1016/j.bcab.2018.11.029
10. [10]
  Mayorgamartinez, C. C.; Gusmao, R.; Sofer, Z.; Pumera, M. Angew. Chem. Int. Ed. 2019, 58, 134. doi: 10.1002/anie.201808846 doi: 10.1002/anie.201808846
11. [11]
  Zhang, G. L.; Pan, X. H.; Kan, J. Q.; Zhang, J. H.; Li, Y. F. Acta Phys. -Chim. Sin. 2003, 19, 533. doi: 10.3866/PKU.WHXB20030611
12. [12]
  He, C. X.; Yuan, A. P.; Zhang, Q. L.; Ren, X. Z.; Li, C. H.; Liu, J. H. Acta Phys. -Chim. Sin. 2012, 28, 2721. doi: 10.3866/PKU.WHXB201207191
13. [13]
  Qiu, Y.; Deng, D.; Deng, Q.; Wu, P.; Zhang, H.; Cai, C. J. Mater. Chem. B 2015, 3, 4487. doi: 10.1039/C5TB00638D doi: 10.1039/C5TB00638D
14. [14]
  Ma, G. X.; Zhong, H.; Lu, T. H.; Xia, Y. Y. Acta Phys. -Chim. Sin. 2007, 23, 1053. doi: 10.3866/PKU.WHXB20070717
15. [15]
  Chen, L.; Yang, G.; Wu, P.; Cai, C. Biosens. Bioelectron. 2017, 96, 294. doi: 10.1016/j.bios.2017.05.022 doi: 10.1016/j.bios.2017.05.022
16. [16]
  Artés, J. M.; Díez-Pérez, I.; Gorostiza, P. Nano Lett. 2012, 12, 2679. doi: 10.1021/nl2028969 doi: 10.1021/nl2028969
17. [17]
  Hayierbiek, K.; Zhao, S. X.; Yang, Y.; Zeng, H. Acta Phys. -Chim. Sin. 2015, 31, 1715. doi: 10.3866/PKU.WHXB201506231
18. [18]
  Zeng H.; Liao, L. W.; Li, M. F.; Tao, Q.; Kang, J.; Chen, Y. X. Acta Phys. -Chim. Sin. 2010, 26, 3217. doi: 10.3866/PKU.WHXB20101208
19. [19]
  Amdursky, N.; Pecht, I.; Sheves, M.; Cahen, D. J. Am. Chem. Soc. 2012, 134, 18221. doi: 10.1021/ja308953q doi: 10.1021/ja308953q
20. [20]
  Amdursky, N.; Ferber, D.; Pecht, I.; Sheves, M.; Cahen, D. Phys. Chem. Chem. Phys. 2013, 15, 17142. doi: 10.1039/C3CP52885E doi: 10.1039/C3CP52885E
21. [21]
  Mentovich, E.; Belgorodsky, B.; Gozin, M.; Richter, S.; Cohen, H. J. Am. Chem. Soc. 2012, 134, 8468. doi: 10.1021/ja211790u doi: 10.1021/ja211790u
22. [22]
  Beilis, E.; Horowitz, Y.; Givon, A.; Somorjai, G.A.; Cohen, H.; Richter, S. J. Phys. Chem. C 2017, 121, 9579. doi: 10.1021/acs.jpcc.7b01355 doi: 10.1021/acs.jpcc.7b01355
23. [23]
  Wang, Q.; Xu, W.; Wu, P.; Zhang, H.; Cai, C.; Zhao, B. J. Phys. Chem. B 2010, 114, 12754. doi: 10.1021/jp106214v doi: 10.1021/jp106214v
24. [24]
  Qian, Y.; Xu, X.; Wang, Q.; Wu, P.; Zhang, H.; Cai, C. Phys. Chem. Chem. Phys. 2013, 15, 16941. doi: 10.1039/C3CP52352G doi: 10.1039/C3CP52352G
25. [25]
  Bera, S.; Kolay, J.; Banerjee, S.; Mukhopadhyay, R. Langmuir 2017, 33, 1951. doi: 10.1021/acs.langmuir.6b04120 doi: 10.1021/acs.langmuir.6b04120
26. [26]
  Rakshit, T.; Mukhopadhyay, R. Langmuir 2011, 27, 9681. doi: 10.1021/la202045a doi: 10.1021/la202045a
27. [27]
  Liang, W.; Wu, C.; Cai, Z.; Sun, Y.; Zhang, H.; Wu, P.; Cai, C. Chem. Commun. 2019, 55, 2853. doi: 10.1039/C9CC00688E doi: 10.1039/C9CC00688E
28. [28]
  Spahr, P. F.; Edsall, J. T. J. Biol. Chem. 1964, 239, 850.
29. [29]
  Castañeda Ocampo, O. E.; Gordiichuk, P.; Catarci, S.; Gautier, D. A.; Herrmann, A.; Chiechi, R. C. J. Am. Chem. Soc. 2015, 137, 8419. doi: 10.1021/jacs.5b01241 doi: 10.1021/jacs.5b01241
30. [30]
  Setty Venkat, A.; Corni, S.; Felice, R. D. Small 2007, 3, 1431. doi: 10.1002/smll.200700001 doi: 10.1002/smll.200700001
31. [31]
  Bujacz, A. Acta Crystallogr. D 2012, 68, 1278. doi: 10.1107/S0907444912027047 doi: 10.1107/S0907444912027047
32. [32]
  Rombouts, I.; Lagrain, B.; Scherf, K. A.; Lambrecht, M. A.; Koehler, P.; Delcour, J. A. Sci. Rep. 2015, 5, 12210. doi: 10.1038/srep12210 doi: 10.1038/srep12210
33. [33]
  Seitz, O.; Vilan, A.; Cohen, H.; Chan, C.; Hwang, J.; Kahn, A. A.; Cahen, D. J. Am. Chem. Soc. 2007, 129, 7494. doi: 10.1021/ja071960p doi: 10.1021/ja071960p
34. [34]
  Chiechi, R. C.; Weiss, E. A.; Dickey, M. D.; Whitesides, G. M. Angew. Chem. Int. Ed. 2008, 47, 142. doi: 10.1002/anie.200703642 doi: 10.1002/anie.200703642
35. [35]
  Adams, P. A.; Berman, M. C. Biochem. J. 1980, 191, 95. doi: 10.1042/bj1910095 doi: 10.1042/bj1910095
36. [36]
  Zunszain, P. A.; Ghuman, J.; Komatsu, T.; Tsuchida, E.; Curry, S. BMC Struct. Biol. 2003, 3, 7. doi: 10.1186/1472-6807-3-7 doi: 10.1186/1472-6807-3-7
37. [37]
  Makarska-Bialokoz, M. Spectrochim. Acta Part A: Mol. Biomol. Spectro. 2018, 193, 23. doi: 10.1016/j.saa.2017.11.063 doi: 10.1016/j.saa.2017.11.063
38. [38]
  Guo, Y.; Deng, L.; Li, J.; Guo, S.; Wang, E.; Dong, S. ACS Nano 2011, 5, 1282. doi: 10.1021/nn1029586 doi: 10.1021/nn1029586
39. [39]
  Xu, X.; Wu, P.; Xu, W.; Shao, Q.; An, L.; Zhang, H.; Cai, C. Phys. Chem. Chem. Phys. 2012, 14, 5824. doi: 10.1039/c2cp24121h doi: 10.1039/c2cp24121h
40. [40]
  Shao, Q.; Wu, P.; Xu, X.; Zhang, H.; Cai, C. Phys. Chem. Chem. Phys. 2012, 14, 9076. doi: 10.1039/c2cp40654c doi: 10.1039/c2cp40654c
41. [41]
  Beilis, E.; Belgorodsky, B.; Fadeev, L.; Cohen, H.; Richter, S. J. Am. Chem. Soc. 2014, 136, 6151. doi: 10.1021/ja410754t doi: 10.1021/ja410754t
42. [42]
  Varnholt, B.; Oulevey, P.; Luber, S.; Kumara, C.; Dass, A.; Burgi, T. J. Phys. Chem. C 2014, 118, 9604. doi: 10.1021/jp502453q doi: 10.1021/jp502453q
43. [43]
  Yamada, T. K.; Bischoff, M. M.; Mizoguchi, T.; van Kempen, H. Surf. Sci. 2002, 516, 179. doi: 10.1016/S0039-6028(02)02032-0 doi: 10.1016/S0039-6028(02)02032-0
44. [44]
  Yamada, T. K.; Bischoff, M. M.; Heijnen, G. M.; Mizoguchi, T.; van Kempen, H. Phys. Rev. Lett. 2003, 90, 056803. doi: 10.1103/PhysRevLett.90.056803 doi: 10.1103/PhysRevLett.90.056803
45. [45]
  Ukraintsev, V. A. Phys. Rev. B 1996, 53, 11176. doi: 10.1103/PhysRevB.53.11176 doi: 10.1103/PhysRevB.53.11176
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