Fibrillogenesis of human serum albumin in the presence of levodopa - spectroscopic, calorimetric and microscopic studies

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• 作者：Mohammad Rehan Ajmal^a ; Tajalli Ilm Chandel^a ; Parvez Alam^a ; Nida Zaidi^a ; Masihuz Zaman^a ; Saima Nusrat^a ; Mohsin Vahid Khan^a ; Mohammad Khursheed Siddiqi^a ; Yasser E. Shahein^b ; Mohamed H. Mahmoud^c ; ^d ; Gamal Badr^e ; Rizwan Hasan Khan^a ; ^{rizwanhkhan1@gmail.com} ; ^{rizwanhkhan1@yahoo.com}
• 关键词：Human serum albumin ; Levodopa ; Thioflavin T ; Isothermal titration calorimetry ; Molecular docking
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：94
• 期：part_PA
• 页码：301-308
• 全文大小：2231 K
• 卷排序：94

文摘

Studying amyloid associated neurodegenerative diseases is an active area of research. Levodopa not only significantly inhibits heat induced fibrillization of human serum albumin but also disaggregates preformed fibrils. Binding of levodopa was studied using isothermal titration calorimetry (ITC), binding constant was found to be 3.6 × 103. Thermal stabilization effect of levodopa on HSA was studied using differential scanning calorimetry (DSC). Microscopic imaging techniques were employed to analyze the morphology of aggregates and effect of levodopa on aggregation.