A multidisciplinary approach to characterize the physicochemical interactions between protein and phenolic ligands.

表征蛋白质和酚类配体之间的物理化学相互作用的多学科方法。

• 批准号: 552698-2020
• 负责人: Mousseau, Normand
• 金额: $ 1.46万
• 依托单位: Université de Montréal
• 依托单位国家: 加拿大
• 项目类别: Alliance Grants
• 财政年份: 2020
• 资助国家: 加拿大
• 起止时间: 2020-01-01 至 2021-12-31
• 项目状态: 已结题
• 来源: https://www.nserc-crsng.gc.ca/ase-oro/Details-Detailles_eng.asp?id=703974
• 关键词: multidisciplinary; approach; characterize; physicochemical; interactions

From a multidisciplinary approach, we will characterize the physicochemical interactions between protein and phenolic ligands, which are playing a major role in many biological processes. These key issues have to be addressed to better understand the biological responses of some natural ligands such as polyphenols. Accumulating data on the protective effects of natural polyphenolic compounds in the progression of neurodegenerative diseases (NDs) has been reported. In this research, we propose a new mechanism to delay the self-association of the protein amyloid-beta (Aß), which could potentially have a positive impact on various biological processes. The amyloid-beta peptide is an endogenous compound which is involved in several pathologies. To test this mechanism, we will combine different multidisciplinary models from theoretical (molecular modelling), experimental (QCMD, real-time nanoparticle tracking) methods and cellular models to better understand the physicochemical interactions between different molecules and their activities.

从多学科的角度，我们将描述蛋白质和酚类配体之间的物理化学相互作用，它们在许多生物过程中发挥着重要作用。必须解决这些关键问题，以便更好地了解一些天然配体(如多酚)的生物反应。关于天然多酚化合物在神经退行性疾病(NDS)进展中的保护作用的数据已有报道。在这项研究中，我们提出了一种新的机制来延缓淀粉样β蛋白(A？)的自关联，这可能对各种生物过程产生积极的影响。淀粉样β蛋白是一种内源性化合物，参与多种病理过程。为了测试这一机制，我们将结合不同的多学科模型，从理论(分子建模)、实验(QCMD，实时纳米粒子跟踪)方法和细胞模型来更好地了解不同分子之间的物理化学相互作用及其活性。