Molecular dynamics simulation of effect of terahertz waves on the secondary structure of potassium channel proteins

Sun Yuan-Kun; Guo Liang-Hao; Wang Kai-Cheng; Wang Shao-Meng; Gong Yu-Bin

doi:10.7498/aps.70.20211725

Abstract

Potassium channels play an important role in repolarizing the nerve cell action potentials. There are many types of potassium channel proteins, and potassium channels allow potassium ions to specifically pass through the cell membrane, thereby maintaining the resting potential of nerve cells. In this paper, molecular dynamics simulation method is used to simulate the effects of 53.7 THz terahertz wave with different amplitudes on the secondary structure of KcsA potassium channel protein and the potassium ions rate. It is found in this study that under the action of the 53.7 THz terahertz wave, the number of alpha helices in KcsA potassium channel protein decreases, and the number of beta sheets and the number of coils increase. In addition, the 53.7 THz terahertz wave can accelerate potassium ions through the KcsA potassium channel. In this article, the effects of terahertz waves on potassium channel proteins are analyzed through the secondary structure of proteins, and a new perspective for the interaction between terahertz waves and biological functional molecules is presented as well.

Keywords:

Authors and contacts

National Key Laboratory of Science and Technology on Vacuum Electronics, School of Electronic Science and Engineering (National Exemplary School of Microelectronics), University of Electronic Science and Technology of China, Chengdu 610054, China

Corresponding author: Gong Yu-Bin, ybgong@uestc.edu.cn

Funds: Project supported by the National Natural Science Foundation of China (Grant No. 61921002) and the National Basic Science Center of National Natural Science Foundation of China (Grant No. 61988102)

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References

[1]	Nelson M T, Quayle J M 1995 Am. J. Physiol. 268 C799 Google Scholar
[2]	Faraci F M, Sobey C G 1996 Clin. Exp. Pharmacol. Physiol. 23 1091 Google Scholar
[3]	Orias M 1998 Medicina 58 429
[4]	Johnston J, Forsythe I D, Kopp-Scheinpflug C 2010 J. Physiol. 588 3187 Google Scholar
[5]	Yellen G 2002 Nature 419 35 Google Scholar
[6]	Guan D, Lee J C F, Higgs M H, Spain W J, Foehring R C 2007 J. Neurophys. 97 1931 Google Scholar
[7]	Guan D, Armstrong W E, Foehring R C 2013 J. Physiol. 591 4807 Google Scholar
[8]	Zhu Z, Cheng C, Chang C, Ren G, Zhang J, Peng Y, Han J, Zhao H 2019 Analyst 144 2504 Google Scholar
[9]	周俊, 刘盛纲 2014 现代应用物理 5 85 Google Scholar Zhou J, Liu S G 2014 Modern Applied Physics 5 85 Google Scholar
[10]	Michele J C, Piero U 2021 Chem. Phys. 155 075102 Google Scholar
[11]	Sizov F 2017 SPQEO 20 273 Google Scholar
[12]	Li N, Peng D L, Zhang X J, Shu Y S, Zhang F, Jiang L, Song B 2021 Nano Res. 14 40 Google Scholar
[13]	Wilmink G J, Grundt J E 2011 J. Infrared Millimeter Terahertz Waves 32 1074 Google Scholar
[14]	Bo W F, Guo L H, Yang Y, Ma J L, Wang K C, Tang J C, Wu Z, Zeng B Q, Gong Y B 2020 IEEE Access 8 10305 Google Scholar
[15]	Li Y M, Chang C, Zhu Z, Sun L, Fan C H 2021 JACS 143 4311 Google Scholar
[16]	Liu X, Qiao Z, Chai Y M, Zhu Z, Wu K J, Ji W L, Li D G, Xiao Y J, Mao L Q, Chang C, Wen Q, Song B, Shu Y S 2021 PNAS 118 e2015685118 Google Scholar
[17]	Zhang J X, He Y, Liang S S, Liao X, Li T, Qiao Z, Chang C, Jia H B, Chen X W 2021 Nat. Commun. 12 2730 Google Scholar
[18]	Zhu Z, Chen C, Chang C, Song B 2021 ACS Photonics 8 781 Google Scholar
[19]	Zhang X X, He M X, Chen Y, Li C, Zhao J W, Wang P F, Peng X 2019 Chin. Phys. B 28 128702 Google Scholar
[20]	Alexandrov B S, Rasmussen K Ø, Bishop A R, Usheva A, Rodriguez G 2011 Biomed. Opt. Express 2 2679 Google Scholar
[21]	Yamazaki S, Harata M, Ueno Y, Tsubouchi M, Konagaya K, Ogawa Y, Isoyama G, Otani C, Hoshina H 2020 Sci. Rep. 10 9008 Google Scholar
[22]	Yamazaki S, Harata M, Idehara T, Konagaya K, Yokoyama G, Hoshina H, Ogawa Y 2018 Sci. Rep. 8 9990 Google Scholar
[23]	Wu K J, Qi C H, Zhu Z, Wang C L, Song B, Chang C 2020 J. Phys. Chem. Lett. 11 7002 Google Scholar
[24]	Takehiro T, Reiko S, Shiho T, Ken-Ichiro K, Hideki H 2020 Opt. Lett. 45 6078 Google Scholar
[25]	Jorgensen W L, Chandrasekhar J, Madura J D, Impey R W, Klein M L 1983 J. Chem. Phys. 79 926 Google Scholar
[26]	Biggin P C, Smith G R, Shrivastava I, Choe S, Sansom M S P 2001 BBA-Biomemberanes 1510 1 Google Scholar
[27]	Berendsen H J C, Spoel D V D, Drunen R V 1995 Comput. Phys. Commun. 91 43 Google Scholar
[28]	Parker M J, Sessions R B, Badcoe I G, Clarke A R 1996 Fold Des. 1 145 Google Scholar
[29]	Zhou H X, Wlodek S T, McCammon J A 1998 PNAS 95 9280 Google Scholar
[30]	Barron L D, Hecht L, Wilson G 1997 Biochemistry 36 13143 Google Scholar
[31]	Fischer S, Smith J C, Verma C S 2001 J. Phys. Chem. B 105 8050 Google Scholar
[32]	Leach A R 2001 Molecular Modelling: Principles and Applications (2nd Ed.) (Harlow: Pearson Education Ltd.) pp20−30
[33]	Rath A, Johnson R M, Deber C M 2007 Pept. Sci. 88 217 Google Scholar
[34]	Moore D T, Berger B W, DeGrado W F 2008 Structure 16 991 Google Scholar
[35]	Matthews E E, Zoonens M, Engelman D M 2006 Cell 127 447 Google Scholar

Cited By

图 1 (a) KcsA四聚体结构(从上往下); (b) KcsA四聚体结构(从前往后); (c)钾离子通道模型

Figure 1. (a) KcsA tetramer structure (from top to bottom); (b) KcsA tetramer structure (from front to back); (c) potassium channel model.

DownLoad: Full-Size Img PowerPoint

图 2 太赫兹波强度不同时钾离子通道蛋白中氢键的变化

Figure 2. Changes of hydrogen bonds in potassium channel proteins at different terahertz intensities.

DownLoad: Full-Size Img PowerPoint

图 3 太赫兹波强度不同时钾离子通道蛋白中二级结构数目的变化

Figure 3. Changes in the number of secondary structures in potassium channel proteins under different terahertz intensities.

DownLoad: Full-Size Img PowerPoint

图 4 太赫兹波强度不同时钾离子通道蛋白中α螺旋数目的变化

Figure 4. Changes in the number of α-helices in potassium channel protein under different terahertz intensities.

DownLoad: Full-Size Img PowerPoint

图 5 太赫兹波强度不同时钾离子通道蛋白中β折叠数目的变化

Figure 5. Changes in the number of β-sheet in potassium channel protein under different terahertz intensities.

DownLoad: Full-Size Img PowerPoint

图 6 太赫兹波强度不同时钾离子通道蛋白中卷曲数目的变化

Figure 6. Changes in the number of coil in potassium channel protein under different terahertz intensities.

DownLoad: Full-Size Img PowerPoint

图 7 太赫兹波强度不同时钾离子通过钾离子通道的数目

Figure 7. Number of potassium ions passing through potassium channels under different intensities of terahertz.

DownLoad: Full-Size Img PowerPoint

[1]	Nelson M T, Quayle J M 1995 Am. J. Physiol. 268 C799 Google Scholar
[2]	Faraci F M, Sobey C G 1996 Clin. Exp. Pharmacol. Physiol. 23 1091 Google Scholar
[3]	Orias M 1998 Medicina 58 429
[4]	Johnston J, Forsythe I D, Kopp-Scheinpflug C 2010 J. Physiol. 588 3187 Google Scholar
[5]	Yellen G 2002 Nature 419 35 Google Scholar
[6]	Guan D, Lee J C F, Higgs M H, Spain W J, Foehring R C 2007 J. Neurophys. 97 1931 Google Scholar
[7]	Guan D, Armstrong W E, Foehring R C 2013 J. Physiol. 591 4807 Google Scholar
[8]	Zhu Z, Cheng C, Chang C, Ren G, Zhang J, Peng Y, Han J, Zhao H 2019 Analyst 144 2504 Google Scholar
[9]	周俊, 刘盛纲 2014 现代应用物理 5 85 Google Scholar Zhou J, Liu S G 2014 Modern Applied Physics 5 85 Google Scholar
[10]	Michele J C, Piero U 2021 Chem. Phys. 155 075102 Google Scholar
[11]	Sizov F 2017 SPQEO 20 273 Google Scholar
[12]	Li N, Peng D L, Zhang X J, Shu Y S, Zhang F, Jiang L, Song B 2021 Nano Res. 14 40 Google Scholar
[13]	Wilmink G J, Grundt J E 2011 J. Infrared Millimeter Terahertz Waves 32 1074 Google Scholar
[14]	Bo W F, Guo L H, Yang Y, Ma J L, Wang K C, Tang J C, Wu Z, Zeng B Q, Gong Y B 2020 IEEE Access 8 10305 Google Scholar
[15]	Li Y M, Chang C, Zhu Z, Sun L, Fan C H 2021 JACS 143 4311 Google Scholar
[16]	Liu X, Qiao Z, Chai Y M, Zhu Z, Wu K J, Ji W L, Li D G, Xiao Y J, Mao L Q, Chang C, Wen Q, Song B, Shu Y S 2021 PNAS 118 e2015685118 Google Scholar
[17]	Zhang J X, He Y, Liang S S, Liao X, Li T, Qiao Z, Chang C, Jia H B, Chen X W 2021 Nat. Commun. 12 2730 Google Scholar
[18]	Zhu Z, Chen C, Chang C, Song B 2021 ACS Photonics 8 781 Google Scholar
[19]	Zhang X X, He M X, Chen Y, Li C, Zhao J W, Wang P F, Peng X 2019 Chin. Phys. B 28 128702 Google Scholar
[20]	Alexandrov B S, Rasmussen K Ø, Bishop A R, Usheva A, Rodriguez G 2011 Biomed. Opt. Express 2 2679 Google Scholar
[21]	Yamazaki S, Harata M, Ueno Y, Tsubouchi M, Konagaya K, Ogawa Y, Isoyama G, Otani C, Hoshina H 2020 Sci. Rep. 10 9008 Google Scholar
[22]	Yamazaki S, Harata M, Idehara T, Konagaya K, Yokoyama G, Hoshina H, Ogawa Y 2018 Sci. Rep. 8 9990 Google Scholar
[23]	Wu K J, Qi C H, Zhu Z, Wang C L, Song B, Chang C 2020 J. Phys. Chem. Lett. 11 7002 Google Scholar
[24]	Takehiro T, Reiko S, Shiho T, Ken-Ichiro K, Hideki H 2020 Opt. Lett. 45 6078 Google Scholar
[25]	Jorgensen W L, Chandrasekhar J, Madura J D, Impey R W, Klein M L 1983 J. Chem. Phys. 79 926 Google Scholar
[26]	Biggin P C, Smith G R, Shrivastava I, Choe S, Sansom M S P 2001 BBA-Biomemberanes 1510 1 Google Scholar
[27]	Berendsen H J C, Spoel D V D, Drunen R V 1995 Comput. Phys. Commun. 91 43 Google Scholar
[28]	Parker M J, Sessions R B, Badcoe I G, Clarke A R 1996 Fold Des. 1 145 Google Scholar
[29]	Zhou H X, Wlodek S T, McCammon J A 1998 PNAS 95 9280 Google Scholar
[30]	Barron L D, Hecht L, Wilson G 1997 Biochemistry 36 13143 Google Scholar
[31]	Fischer S, Smith J C, Verma C S 2001 J. Phys. Chem. B 105 8050 Google Scholar
[32]	Leach A R 2001 Molecular Modelling: Principles and Applications (2nd Ed.) (Harlow: Pearson Education Ltd.) pp20−30
[33]	Rath A, Johnson R M, Deber C M 2007 Pept. Sci. 88 217 Google Scholar
[34]	Moore D T, Berger B W, DeGrado W F 2008 Structure 16 991 Google Scholar
[35]	Matthews E E, Zoonens M, Engelman D M 2006 Cell 127 447 Google Scholar

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