来自SARS-CoV-2 S1,S2,RBD和N重组蛋白的自组合的粉样样纳米结构
Olga V Morozova1, Valentin A Manuvera2, Nikolay A Barinov3
1Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency, 1a Malaya Pirogovskaya Street, 119435, Moscow, Russian Federation; Ivanovsky Institute of Virology of the National Research Center of Epidemiology and Microbiology of N.F. Gamaleya of the Russian Ministry of Health, 16 Gamaleya Street, 123098, Moscow, Russian Federation; Moscow Institute of Physics and Technology, 9 Institutsky Per., 141700, Dolgoprudny, Moscow Region, Russian Federation; Sirius University of Science and Technology, Olimpiyskiy ave. b.1, township Sirius, Krasnodar region, 354340, Russian Federation.
来自SARS-CoV-2蛋白质的自组装纳米颗粒自发形成粉样结构,可能导致蛋白质病变并影响疫苗的稳定性. 这些纳米结构表现出稳定性和受体介导的细胞进入.
科学领域:
- 生物物理学的生物物理.
- 纳米技术纳米技术
- 病毒学 病毒学
背景情况:
- 研究了SARS-CoV-2的重组蛋白 (S1,S2,RBD,N) 进行自我组装.
- 了解病毒蛋白的结构性质对于疫苗开发和疾病的发病至关重要.
研究的目的:
- 描述由SARS-CoV-2蛋白质形成的自组装纳米粒子 (saNP).
- 研究这些saNP的稳定性,结构和细胞相互作用.
- 探索这些粉样样纳米结构在疾病和诊断方面的潜在影响.
主要方法:
- 通过亲和染色学净化蛋白质.
- 使用扫描电子显微镜 (SEM),原子力显微镜 (AFM) 和动态光散射 (DLS) 进行纳米结构表征.
- 在各种条件下的稳定性评估和细胞透研究.
主要成果:
- SARS-CoV-2 蛋白质自发形成固体,粉样类 saNP 和纳米纤维.
- 飞行机组显示了S1,S2,N和RBD saNP的不同平均高度.
- saNP表现出随时间的推移和结解周期的稳定性,具有高效的受体介导进入特定细胞.
结论:
- 从SARS-CoV-2蛋白质中自发形成粉样saNP被证实.
- 这些纳米结构可能会导致蛋白质病变,包括神经退行性疾病.
- 研究结果表明,这可能会对疫苗稳定性和诊断系统产生影响.
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