公共化学
蛋白质数据库
双氯西林
蛋白质数据库
抗生素
化学
金黄色葡萄球菌
抗菌活性
对接(动物)
配体(生物化学)
细菌
蛋白质结构
生物化学
生物
医学
受体
兽医学
遗传学
氨苄西林
作者
K. Meghana,S. Sivaprasad
标识
DOI:10.18137/cardiometry.2022.25.16131619
摘要
Aim: The goal is to compare the antibacterial properties of carbohydrates derivates to those of commercial antibiotics, using docking to see how the ligand, protein, and antibiotic interact molecularly. Materials and procedures: The PDB (protein data bank) website was used to obtain the protein structure, whereas the NCBI-PubChem website was used to gain the ligand structure. The three different types of chemicals used for docking include antibacterial from Staphylococcus aureus(1N67), gluconolactone as a ligand, and dicloxacillin as an antibiotic. The PubChem website contains the true nature of protein chemical structure, while the PDB website has the chemical structures of ligand and antibiotic. The goal was to see if the interaction between the antibacterial staphylococcus aureus (1N67) protein molecule and the antibiotic dicloxacillin was right. Using SPSS software, the independent sample t-test was employed to compare binding affinity. According to statistics, one-sided p values range from.18 to.001, whereas two-sided p values range from.345 to.001. Conclusion: When it comes to antibacterial activity against the target protein, the antibiotic dicloxacillin appears to be more specific and selective.
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