Alam Parvez, Siddiqi Mohammad Khursheed, Chaturvedi Sumit Kumar, Zaman Masihuz, Khan Rizwan Hasan
Molecular Biophysics and Biophysical Chemistry Group, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, India.
Molecular Biophysics and Biophysical Chemistry Group, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, 202002, India.
Int J Biol Macromol. 2017 Jun;99:477-482. doi: 10.1016/j.ijbiomac.2017.03.001. Epub 2017 Mar 4.
Protein misfolding and aggregation has been implicated as the cause of more than 20 diseases in humans such as Alzheimer's and Parkinson's and systemic amyloidosis. Retardation of Aβ- 42 aggregation is considered as a promising and challenging strategy for developing effective therapeutics against Alzheimer's disease. Herein, we demonstrated the effect of vitamin B12 (VB) on inhibiting amyloid formation by employing ThT fluorescence assay, circular dichroism, ANS fluorescence assay, dynamic light scattering measurements and transmission electron microscopy and cell viability assay. Our results demonstrate that vitamin B12 (VB), inhibits Aβ- 42 aggregation in a concentration dependent manner. Further VB also provide protection against amyloid induced cytotoxicity in human neuronal cell line. This study points towards a promising strategy to combat Aβ- 42 aggregation and may have broader implication for targeting other neurological disorders whose distinct hallmark is also amyloid formation.
蛋白质错误折叠和聚集被认为是导致人类20多种疾病的原因,如阿尔茨海默病、帕金森病和系统性淀粉样变性。抑制Aβ-42聚集被认为是开发针对阿尔茨海默病的有效治疗方法的一种有前景且具有挑战性的策略。在此,我们通过噻唑蓝(ThT)荧光测定、圆二色性、ANS荧光测定、动态光散射测量、透射电子显微镜和细胞活力测定,证明了维生素B12(VB)对抑制淀粉样蛋白形成的作用。我们的结果表明,维生素B12(VB)以浓度依赖的方式抑制Aβ-42聚集。此外,VB还能保护人类神经元细胞系免受淀粉样蛋白诱导的细胞毒性。这项研究指出了一种对抗Aβ-42聚集的有前景的策略,可能对针对其他以淀粉样蛋白形成为显著特征的神经疾病具有更广泛的意义。