Citation: Zhen LIANG, Wen-Li YAN, Hong-Mei LI, Ying LI, Rong ZHANG. Studies on the Molecular Mechanism between HDAC8 and Inhibitory in Different Bioactivities by Molecular Docking and MD Simulations[J]. Chinese Journal of Structural Chemistry, ;2021, 40(10): 1298-1308. doi: 10.14102/j.cnki.0254–5861.2011–3126 shu

Studies on the Molecular Mechanism between HDAC8 and Inhibitory in Different Bioactivities by Molecular Docking and MD Simulations

School of Pharmacy, Guangdong Pharmaceutical University, Guangzhou 510006, China

Corresponding author: Rong ZHANG, zhangr@gdpu.edu.cn
Received Date: 29 January 2021
Accepted Date: 12 April 2021

Fund Project: Talents Introduction Foundation for Universities of Guangdong Province GD 2011the Science and Technology Planning Project of Guangzhou 2013J4100071

Figures(11)

HDAC8 is an important target for the treatment of many cancers and other diseases. To develop potent and selective HDAC8 inhibitors, molecular docking and molecular dynamics (MD) simulations were employed for investigation of the mechanism of HDAC8 inhibitions containing hydroxamic acid group. Compound 1 with high activity and compound 2 with low activity were selected for comparative study. Compound 1 formed a stronger chelation with Zn ion and was more stable in the HDAC8 pocket than compound 2. Residues HIS-180, ASP-178, ASP-267, and GLY-140 played a critical role in securing the position of compound 1. Both the head and tail of compound 1 formed strong hydrogen bonds with ASP-178, facilitating the ZBG of compound 1 close to the Zn ion so that they formed permanent chelation during the simulation period. The Cap group of the compounds with branch and long chains was advantageous to form interaction with active pocket opening. What's more, based on the results of this study, three innovative recommendations for the design of highly active HDAC8 inhibitors were presented, which will be useful for the development of new HDAC8 inhibitors.
- HDAC8 inhibitors,
- molecular docking,
- molecular dynamics (MD) simulations,
- inhibition mechanism
1. [1]
  Amin, S. A.; Adhikari, N.; Jha, T. Diverse classes of HDAC8 inhibitors: in search of molecular fingerprints that regulate activity. Future Med. Chem. 2018, 10, 1589−1602. doi: 10.4155/fmc-2018-0005
2. [2]
  Amin, S. A.; Adhikari, N.; Jha, T. Is dual inhibition of metalloenzymes HDAC-8 and MMP-2 a potential pharmacological target to combat hematological malignancies? Pharmacol Res. 2017, 122, 8−19. doi: 10.1016/j.phrs.2017.05.002
3. [3]
  Amin, S. A.; Adhikari, N.; Jha, T. Structure-activity relationships of hydroxamate-based histone deacetylase-8 inhibitors: reality behind anticancer drug discovery. Future Med. Chem. 2017, 9, 2211−2237. doi: 10.4155/fmc-2017-0130
4. [4]
  Halder, A. K.; Mallick, S.; Shikha, D.; Saha, A.; Saha, K. D.; Jha, T. Design of dual MMP-2/HDAC-8 inhibitors by pharmacophore mapping, molecular docking, synthesis and biological activity. RSC Adv. 2015, 5, 72373−72386. doi: 10.1039/C5RA12606A
5. [5]
  Buggy, J. J.; Sideris, M. L.; Mak, P.; Lorimer, D. D.; McIntosh, B.; Clark, J. M. Cloning and characterization of a novel human histone deacetylase, HDAC8. Biochem. J. 2000, 199−205.
6. [6]
  Li, J.; Chen, S.; Cleary, R. A.; Wang, R.; Gannon, O. J.; Seto, E.; Tang, D. D. Histone deacetylase 8 regulates cortactin deacetylation and contraction in smooth muscle tissues. Am. J. Physiol. Cell Physiol. 2014, 307, 288−295. doi: 10.1152/ajpcell.00102.2014
7. [7]
  Hu, E.; Chen, Z.; Fredrickson, T.; Zhu, Y.; Kirkpatrick, R.; Zhang, G. F.; Johanson, K.; Sung, C. M.; Liu, R.; Winkler, J. Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. J. Biol. Chem. 2000, 275, 15254−15264. doi: 10.1074/jbc.M908988199
8. [8]
  Chakrabarti, A.; Oehme, I.; Witt, O.; Oliveira, G.; Sippl, W.; Romier, C.; Pierce, R. J.; Jung, M. HDAC8: a multifaceted target for therapeutic interventions. Trends Pharmacol Sci. 2015, 36, 481−492. doi: 10.1016/j.tips.2015.04.013
9. [9]
  Somoza, J. R.; Skene, R. J.; Katz, B. A.; Mol, C.; Ho, J. D.; Jennings, A. J.; Luong, C.; Arvai, A.; Buggy, J. J.; Chi, E.; Tang, J.; Sang, B. C.; Verner, E.; Wynands, R.; Leahy, E. M.; Dougan, D. R.; Snell, G.; Navre, M.; Knuth, M. W.; Swanson, R. V.; McRee, D. E.; Tari, L. W. Structural snapshots of human HDAC8 provide insights into the class I histone deacetylases. Structure 2004, 12, 1325−1334. doi: 10.1016/j.str.2004.04.012
10. [10]
  Nongonierma, A. B.; Dellafiora, L.; Paolella, S.; Galaverna, G.; Cozzini, P.; FitzGerald, R. J. In silico approaches applied to the study of peptide analogs of Ile-Pro-Ile in relation to their dipeptidyl peptidase IV inhibitory properties. Front. Endocrinol. 2018, 9, 329−329. doi: 10.3389/fendo.2018.00329
11. [11]
  Nakagawa, M.; Oda, Y.; Eguchi, T.; Aishima, S.; Yao, T.; Hosoi, F.; Basaki, Y.; Ono, M.; Kuwano, M.; Tanaka, M.; Tsuneyoshi, M. Expression profile of class I histone deacetylases in human cancer tissues. Oncol. Rep. 2007, 18, 769−774.
12. [12]
  Thoma, R.; Löffler, B.; Stihle, M.; Huber, W.; Ruf, A.; Hennig, M. Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV. Structure 2003, 11, 947−959. doi: 10.1016/S0969-2126(03)00160-6
13. [13]
  Adhikari, N.; Amin, S. A.; Trivedi, P.; Jha, T.; Ghosh, B. HDAC3 is a potential validated target for cancer: an overview on the benzamide-based selective HDAC3 inhibitors through comparative SAR/QSAR/QAAR approaches. Eur. J. Med. Chem. 2018, 157, 1127−1142. doi: 10.1016/j.ejmech.2018.08.081
14. [14]
  Wu, J.; Du, C.; Lv, Z.; Ding, C.; Cheng, J.; Xie, H.; Zhou, L.; Zheng, S. The up-regulation of histone deacetylase 8 promotes proliferation and inhibits apoptosis in hepatocellular carcinoma. Dig. Dis. Sci. 2013, 58, 3545−3553. doi: 10.1007/s10620-013-2867-7
15. [15]
  Suzuki, T.; Muto, N.; Bando, M.; Itoh, Y.; Masaki, A.; Ri, M.; Ota, Y.; Nakagawa, H.; Iida, S.; Shirahige, K.; Miyata, N. Design, synthesis, and biological activity of NCC149 derivatives as histone deacetylase 8-selective inhibitors. ChemMedChem. 2014, 9, 657−664. doi: 10.1002/cmdc.201300414
16. [16]
  Qi, J.; Singh, S.; Hua, W. K.; Cai, Q.; Chao, S. W.; Li, L.; Liu, H.; Ho, Y.; McDonald, T.; Lin, A.; Marcucci, G.; Bhatia, R.; Huang, W. J.; Chang, C. I.; Kuo, Y. H. HDAC8 inhibition specifically targets inv(16) acute myeloid leukemic stem cells by restoring p53 acetylation. Cell Stem. Cell. 2015, 17, 597−610. doi: 10.1016/j.stem.2015.08.004
17. [17]
  Nian, H.; Bisson, W. H.; Dashwood, W. M.; Pinto, J. T.; Dashwood, R. H. Alpha-keto acid metabolites of organoselenium compounds inhibit histone deacetylase activity in human colon cancer cells. Carcinogenesis 2009, 30, 1416−1423. doi: 10.1093/carcin/bgp147
18. [18]
  Hsieh, C. L.; Ma, H. P.; Su, C. M.; Chang, Y. J.; Hung, W. Y.; Ho, Y. S.; Huang, W. J.; Lin, R. K. Alterations in histone deacetylase 8 lead to cell migration and poor prognosis in breast cancer. Life Sci. 2016, 151, 7−14. doi: 10.1016/j.lfs.2016.02.092
19. [19]
  Wang, Y.; Xu, P.; Yao, J.; Yang, R.; Shi, Z.; Zhu, X.; Feng, X.; Gao, S. MicroRNA-216b is down-regulated in human gastric adenocarcinoma and inhibits proliferation and cell cycle progression by targeting oncogene HDAC8. Target. Oncol. 2016, 11, 197−207. doi: 10.1007/s11523-015-0390-9
20. [20]
  Oehme, I.; Deubzer, H. E.; Wegener, D.; Pickert, D.; Linke, J. P.; Hero, B.; Kopp-Schneider, A.; Westermann, F.; Ulrich, S. M.; von Deimling, A.; Fischer, M.; Witt, O. Histone deacetylase 8 in neuroblastoma tumorigenesis. Clin. Cancer Res. 2009, 15, 91−99. doi: 10.1158/1078-0432.CCR-08-0684
21. [21]
  Tian, Y.; Wong, V. W.; Wong, G. L.; Yang, W.; Sun, H.; Shen, J.; Tong, J. H.; Go, M. Y.; Cheung, Y. S.; Lai, P. B.; Zhou, M.; Xu, G.; Huang, T. H.; Yu, J.; To, K. F.; Cheng, A. S.; Chan, H. L. Histone deacetylase HDAC8 promotes insulin resistance and β-catenin activation in NAFLD-associated hepatocellular carcinoma. Cancer Res. 2015, 75, 4803−4816.
22. [22]
  Klebe, G.; Abraham, U.; Mietzner, T. Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity. J. Med. Chem. 1994, 37, 4130−4146. doi: 10.1021/jm00050a010
23. [23]
  Doenhoff, M. J.; Cioli, D.; Utzinger, J. Praziquantel: mechanisms of action, resistance and new derivatives for schistosomiasis. Curr. Opin. Infect. Dis. 2008, 21, 659−667. doi: 10.1097/QCO.0b013e328318978f
24. [24]
  Heimburg, T.; Chakrabarti, A.; Lancelot, J.; Marek, M.; Melesina, J.; Hauser, A. T.; Shaik, T. B.; Duclaud, S.; Robaa, D.; Erdmann, F.; Schmidt, M.; Romier, C.; Pierce, R. J.; Jung, M.; Sippl, W. Structure-based design and synthesis of novel inhibitors targeting HDAC8 from schistosoma mansoni for the treatment of schistosomiasis. J. Med. Chem. 2016, 59, 2423−2435. doi: 10.1021/acs.jmedchem.5b01478
25. [25]
  Xia, B.; Lu, J.; Wang, R.; Yang, Z.; Zhou, X.; Huang, P. MiR-21-3p regulates influenza a virus replication by targeting histone deacetylase-8. Front Cell Infect. Microbiol. 2018, 8, 175−175. doi: 10.3389/fcimb.2018.00175
26. [26]
  Meng, J.; Liu, X.; Zhang, P.; Li, D.; Xu, S.; Zhou, Q.; Guo, M.; Huai, W.; Chen, X.; Wang, Q.; Li, N.; Cao, X. Rb selectively inhibits innate IFN-β production by enhancing deacetylation of IFN-β promoter through HDAC1 and HDAC8. J. Autoimmun. 2016, 73, 42−53. doi: 10.1016/j.jaut.2016.05.012
27. [27]
  Jackson, L.; Kline, A. D.; Barr, M. A.; Koch, S. De Lange syndrome: a clinical review of 310 individuals. Am. J. Med. Genet. 1993, 47, 940−946. doi: 10.1002/ajmg.1320470703
28. [28]
  Ingham, O. J.; Paranal, R. M.; Smith, W. B.; Escobar, R. A.; Yueh, H.; Snyder, T.; Porco, J. A., J.; Bradner, J. E.; Beeler, A. B. Development of a potent and selective HDAC8 inhibitor. ACS Med. Chem. Lett. 2016, 7, 929−932. doi: 10.1021/acsmedchemlett.6b00239
29. [29]
  Hassanzadeh, M.; Bagherzadeh, K.; Amanlou, M. A comparative study based on docking and molecular dynamics simulations over HDAC-tubulin dual inhibitors. J. Mol. Graph. Model. 2016, 70, 170−180. doi: 10.1016/j.jmgm.2016.10.007
30. [30]
  Dar, K. B.; Bhat, A. H.; Amin, S.; Hamid, R.; Anees, S.; Anjum, S.; Reshi, B. A.; Zargar, M. A.; Masood, A.; Ganie, S. A. Modern computational strategies for designing drugs to curb human diseases: a prospect. Curr. Top Med. Chem. 2018, 18, 2702−2719.
31. [31]
  Zhou, H.; Wang, C.; Deng, T.; Tao, R.; Li, W. Novel urushiol derivatives as HDAC8 inhibitors: rational design, virtual screening, molecular docking and molecular dynamics studies. J. Biomol. Struct. Dyn. 2018, 36, 1966−1978. doi: 10.1080/07391102.2017.1344568
32. [32]
  Uba, A. I.; Weako, J.; Keskin, Ö.; Gürsoy, A.; Yelekçi, K. Examining the stability of binding modes of the co-crystallized inhibitors of human HDAC8 by molecular dynamics simulation. J. Biomol. Struct. Dyn. 2020, 38, 1751−1760.
33. [33]
  Zhang, Y.; Feng, J.; Jia, Y.; Wang, X.; Zhang, L.; Liu, C.; Fang, H.; Xu, W. Development of tetrahydroisoquinoline-based hydroxamic acid derivatives: potent histone deacetylase inhibitors with marked in vitro and in vivo antitumor activities. J. Med. Chem. 2011, 54, 2823−2838. doi: 10.1021/jm101605z
34. [34]
  Zhang, Y. J.; Feng, J. H.; Liu, C. X.; Fang, H.; Xu, W. F. Design, synthesis and biological evaluation of tyrosine-based hydroxamic acid analogs as novel histone deacetylases (HDACs) inhibitors. Bioorg. Med. Chem. 2011, 19, 4437−4444. doi: 10.1016/j.bmc.2011.06.046
35. [35]
  Zhang, Y. J.; Feng, J. H.; Liu, C. X.; Zhang, L.; Jiao, J.; Fang, H.; Su, L.; Zhang, X. P.; Zhang, J.; Li, M. Y.; Wang, B. H.; Xu, W. F. Design, synthesis and preliminary activity assay of 1, 2, 3, 4-tetrahydroisoquinoline-3-carboxylic acid derivatives as novel histone deacetylases (HDACs) inhibitors. Bioorg. Med. Chem. Lett. 2010, 18, 1761−1772. doi: 10.1016/j.bmc.2010.01.060
36. [36]
  Pidugu, V. R.; Yarla, N. S.; Pedada, S. R.; Kalle, A. M.; Satya, A. K. Design and synthesis of novel HDAC8 inhibitory 2, 5-disubstituted-1, 3, 4-oxadiazoles containing glycine and alanine hybrids with anti cancer activity. Bioorg. Med. Chem. 2016, 24, 5611−5617. doi: 10.1016/j.bmc.2016.09.022
37. [37]
  Qi, C. Y.; Zhang, R.; Liu, F. Z.; Zheng, T.; Wu, W. J. Molecular mechanism of interactions between inhibitory tripeptide GEF and angiotensin-converting enzyme in aqueous solutions by molecular dynamic simulations. J. Mol. Liq. 2018, 249, 389−396. doi: 10.1016/j.molliq.2017.11.033
38. [38]
  Yan, W. L.; Lin, G. M.; Zhang, R.; Liang, Z.; Wu, W. J. Studies on the bioactivities and molecular mechanism of antioxidant peptides by 3D-QSAR, in vitro evaluation and molecular dynamic simulations. Food Funct. 2020, 11, 3043−3052. doi: 10.1039/C9FO03018B
39. [39]
  Tabackman, A. A.; Frankson, R.; Marsan, E. S.; Perry, K.; Cole, K. E. Structure of 'linkerless' hydroxamic acid inhibitor-HDAC8 complex confirms the formation of an isoform-specific subpocket. J. Struct. Biol. 2016, 195, 373−378. doi: 10.1016/j.jsb.2016.06.023
40. [40]
  Lombardi, P. M.; Cole, K. E.; Dowling, D. P.; Christianson, D. W. Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes. Curr. Opin. Struct. Biol. 2011, 21, 735−743. doi: 10.1016/j.sbi.2011.08.004
41. [41]
  Deschamps, N.; Simões-Pires, C. A.; Carrupt, P. A.; Nurisso, A. How the flexibility of human histone deacetylases influences ligand binding: an overview. Drug Discov. Today 2015, 20, 736−742. doi: 10.1016/j.drudis.2015.01.004
42. [42]
  Nechay, M. R.; Gallup, N. M.; Morgenstern, A.; Smith, Q. A.; Eberhart, M. E.; Alexandrova, A. N. Histone deacetylase 8: characterization of physiological divalent metal catalysis. J. Phys. Chem. B 2016, 120, 5884−5895. doi: 10.1021/acs.jpcb.6b00997
1. [1]
  Huanyu Liu , Gang Yu , Ruoyao Guo , Hao Qi , Jiayin Zheng , Tong Jin , Zifeng Zhao , Zuqiang Bian , Zhiwei Liu . Direct identification of energy transfer mechanism in Ce^Ⅲ-Mn^Ⅱ system by constructing molecular heteronuclear complexes. Chinese Chemical Letters, 2025, 36(2): 110296-. doi: 10.1016/j.cclet.2024.110296
2. [2]
  Fang-Yuan Chen , Wen-Chao Geng , Kang Cai , Dong-Sheng Guo . Molecular recognition of cyclophanes in water. Chinese Chemical Letters, 2024, 35(5): 109161-. doi: 10.1016/j.cclet.2023.109161
3. [3]
  Caihong Mao , Yanfeng He , Xiaohan Wang , Yan Cai , Xiaobo Hu . Synthesis and molecular recognition characteristics of a tetrapodal benzene cage. Chinese Chemical Letters, 2024, 35(8): 109362-. doi: 10.1016/j.cclet.2023.109362
4. [4]
  Cheng-Da Zhao , Huan Yao , Shi-Yao Li , Fangfang Du , Li-Li Wang , Liu-Pan Yang . Amide naphthotubes: Biomimetic macrocycles for selective molecular recognition. Chinese Chemical Letters, 2024, 35(4): 108879-. doi: 10.1016/j.cclet.2023.108879
5. [5]
  Yanwei Duan , Qing Yang . Molecular targets and their application examples for interrupting chitin biosynthesis. Chinese Chemical Letters, 2025, 36(4): 109905-. doi: 10.1016/j.cclet.2024.109905
6. [6]
  Zhimin Sun , Xin-Hui Guo , Yue Zhao , Qing-Yu Meng , Li-Juan Xing , He-Lue Sun . Dynamically switchable porphyrin-based molecular tweezer for on−off fullerene recognition. Chinese Chemical Letters, 2024, 35(6): 109162-. doi: 10.1016/j.cclet.2023.109162
7. [7]
  Li Lin , Song-Lin Tian , Zhen-Yu Hu , Yu Zhang , Li-Min Chang , Jia-Jun Wang , Wan-Qiang Liu , Qing-Shuang Wang , Fang Wang . Molecular crowding electrolytes for stabilizing Zn metal anode in rechargeable aqueous batteries. Chinese Chemical Letters, 2024, 35(7): 109802-. doi: 10.1016/j.cclet.2024.109802
8. [8]
  Minghao Hu , Tianci Xie , Yuqiang Hu , Longjie Li , Ting Wang , Tongbo Wu . Allosteric DNAzyme-based encoder for molecular information transfer. Chinese Chemical Letters, 2024, 35(7): 109232-. doi: 10.1016/j.cclet.2023.109232
9. [9]
  Chuan-Zhi Ni , Ruo-Ming Li , Fang-Qi Zhang , Qu-Ao-Wei Li , Yuan-Yuan Zhu , Jie Zeng , Shuang-Xi Gu . A chiral fluorescent probe for molecular recognition of basic amino acids in solutions and cells. Chinese Chemical Letters, 2024, 35(10): 109862-. doi: 10.1016/j.cclet.2024.109862
10. [10]
  Wei-Jia Wang , Kaihong Chen . Molecular-based porous polymers with precise sites for photoreduction of carbon dioxide. Chinese Chemical Letters, 2025, 36(1): 109998-. doi: 10.1016/j.cclet.2024.109998
11. [11]
  Dongpu Wu , Zheng Yang , Yuchen Xia , Lulu Wu , Yingxia Zhou , Caoyuan Niu , Puhui Xie , Xin Zheng , Zhanqi Cao . Surface controllable wettability using amphiphilic rotaxane molecular shuttles. Chinese Chemical Letters, 2025, 36(2): 110353-. doi: 10.1016/j.cclet.2024.110353
12. [12]
  Bingwei Wang , Yihong Ding , Xiao Tian . Benchmarking model chemistry composite calculations for vertical ionization potential of molecular systems. Chinese Chemical Letters, 2025, 36(2): 109721-. doi: 10.1016/j.cclet.2024.109721
13. [13]
  Kai Ye , Zhicheng Ye , Chuantao Wang , Zhilai Luo , Cheng Lian , Chunyan Bao . Artificial signal transduction triggered by molecular photoisomerization in lipid membranes. Chinese Chemical Letters, 2025, 36(4): 110033-. doi: 10.1016/j.cclet.2024.110033
14. [14]
  Man Wu , Chuandong Jia . A light-powered molecular pump achieving transmembrane concentration gradient. Chinese Journal of Structural Chemistry, 2025, 44(4): 100452-100452. doi: 10.1016/j.cjsc.2024.100452
15. [15]
  Qihan Lin , Jiabin Xing , Yue-Yang Liu , Gang Wu , Shi-Jia Liu , Hui Wang , Wei Zhou , Zhan-Ting Li , Dan-Wei Zhang . taBOX: A water-soluble tetraanionic rectangular molecular container for conjugated molecules and taste masking for berberine and palmatine. Chinese Chemical Letters, 2024, 35(5): 109119-. doi: 10.1016/j.cclet.2023.109119
16. [16]
  Zhikang Wu , Guoyong Dai , Qi Li , Zheyu Wei , Shi Ru , Jianda Li , Hongli Jia , Dejin Zang , Mirjana Čolović , Yongge Wei . POV-based molecular catalysts for highly efficient esterification of alcohols with aldehydes as acylating agents. Chinese Chemical Letters, 2024, 35(8): 109061-. doi: 10.1016/j.cclet.2023.109061
17. [17]
  Jinyan Zhang , Fen Liu , Qian Jin , Xueyi Li , Qiong Zhan , Mu Chen , Sisi Wang , Zhenlong Wu , Wencai Ye , Lei Wang . Discovery of unusual phloroglucinol–triterpenoid adducts from Leptospermum scoparium and Xanthostemon chrysanthus by building blocks-based molecular networking. Chinese Chemical Letters, 2024, 35(6): 108881-. doi: 10.1016/j.cclet.2023.108881
18. [18]
  Zixi Zou , Jingyuan Wang , Yian Sun , Qian Wang , Da-Hui Qu . Controlling molecular assembly on time scale: Time-dependent multicolor fluorescence for information encryption. Chinese Chemical Letters, 2024, 35(7): 108972-. doi: 10.1016/j.cclet.2023.108972
19. [19]
  Ruonan Guo , Heng Zhang , Changsheng Guo , Ningqing Lv , Beidou Xi , Jian Xu . Degradation of neonicotinoids with different molecular structures in heterogeneous peroxymonosulfate activation system through different oxidation pathways. Chinese Chemical Letters, 2024, 35(9): 109413-. doi: 10.1016/j.cclet.2023.109413
20. [20]
  Qinghong Pan , Huafang Zhang , Qiaoling Liu , Donghong Huang , Da-Peng Yang , Tianjia Jiang , Shuyang Sun , Xiangrong Chen . A self-powered cathodic molecular imprinting ultrasensitive photoelectrochemical tetracycline sensor via ZnO/C photoanode signal amplification. Chinese Chemical Letters, 2025, 36(1): 110169-. doi: 10.1016/j.cclet.2024.110169

Get Citation

PDF

XML

Metrics

PDF Downloads(4)
Abstract views(1419)
HTML views(7)

通讯作者: 陈斌, bchen63@163.com

1.
沈阳化工大学材料科学与工程学院沈阳 110142