Analysis of damaging non-synonymous SNPs in GPx1 gene associated with the progression of diverse cancers through a comprehensive in silico approach

被引:2
作者
Iqbal, Muhammad Waleed [1 ,2 ]
Shahab, Muhammad [1 ,2 ]
Zheng, Guojun [1 ,2 ]
Sun, Xinxiao [1 ,2 ]
Yuan, Qipeng [1 ,2 ]
Almaary, Khalid S. [3 ]
Wondmie, Gezahign Fentahun [4 ]
Bourhia, Mohammed [5 ]
机构
[1] Beijing Univ Chem Technol, State Key Lab Chem Resources Engn, Beijing 100029, Peoples R China
[2] Beijing Univ Chem Technol, Coll Life Sci & Technol, Beijing 100029, Peoples R China
[3] King Saud Univ, Coll Sci, Dept Bot & Microbiol, POB 2455, Riyadh 11451, Saudi Arabia
[4] Bahir Dar Univ, Dept Biol, POB 79, Bahir Dar, Ethiopia
[5] Ibn Zohr Univ, Fac Sci, Lab Biotechnol & Nat Resources Valorizat, Agadir 80060, Morocco
来源
SCIENTIFIC REPORTS | 2024年 / 14卷 / 01期
关键词
GPx1; Cancer; NsSNPs; Mutational analysis; In-silico analysis; SINGLE NUCLEOTIDE POLYMORPHISMS; GLUTATHIONE-PEROXIDASE; PROTEIN-PHOSPHORYLATION; WEB SERVER; PREDICTION; OVEREXPRESSION; INTEGRATION; MUTATIONS; RS1050450; PROGNOSIS;
D O I
10.1038/s41598-024-78232-6
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Glutathione Peroxidase 1 (GPx1) gene has been reported for its role in cellular redox homeostasis, and the dysregulation of its expression is linked with the progression of diverse cancers. Non-synonymous single nucleotide polymorphism (nsSNPs) have been emerged as the crucial factors, playing their role in GPx1 overexpression. To understand the deleterious mutational effects on the structure and function of GPx1 enzyme, we delved deeper into the exploration of possibly damaging nsSNPs using in-silico based approaches. Eight widely utilized computational tools were employed to roughly shortlist the deleterious nsSNPs. Their damaging effects on structure and function of the genes were evaluated by using different bioinformatics tools. Subsequently, the three final proposed deleterious mutants including mutations rs373838463, rs2107818892, and rs763687242, were docked with their reported binder, TNF receptor-associated factor 2 (TRAF2). The lowest binding affinity and stability of the docked mutant complexes as compared to the wild type GPx1 were validated by molecular dynamic simulation. Finally, the comparison of RMSD, RMSF, RoG and hydrogen bond analyses between wild-type and mutant's complexes validated the deleterious effects of proposed nsSNPs. This study successfully identified and verified the possibly damaging nsSNPs in GPx1 enzyme, which may be linked the progression of various types of cancer. Our findings underscore the value of in-silico approaches in mutational analysis and encourage further preclinical and clinical trials.
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页数:20
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