首页 | 本学科首页   官方微博 | 高级检索  
     


Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study
Authors:Javed Masood Khan  Mohd Shahnawaz Khan  Mohammad Abdulrahman Alsenaidy  Anwar Ahmed  Priyankar Sen  Mohammad Oves
Affiliation:1. Faculty of Food and Agricultural Sciences, Department of Food Science and Nutrition, King Saud University, 2460 Riyadh 11451, Saudi Arabia;2. Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia;3. Department of Pharmaceutics, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia;4. Centre for Bioseparation Technology, VIT University, Vellore 632014, India;5. Center of Excellence in Enviromental Studies, King Abdulaziz University, Jeddah, Saudi Arabia
Abstract:Amyloid fibril formation is responsible for several neurodegenerative diseases and are formed when native proteins misfold and stick together with different interactive forces. In the present study, we have determined the mode of interaction of the anionic surfactant sarkosyl with hen egg white lysozyme (HEWL) [EC No. 3.2.1.17] at two pHs (9.0 and 13.0) and investigated its impact on fibrillogenesis. Our data suggested that sarkosyl is promoting amyloid fibril formation in HEWL at the concentration range between 0.9 and 3.0 mM and no amyloid fibril formation was observed in the concentration range of 3.0–20.0 mM at pH 9.0. The results were confirmed by several biophysical and computational techniques, such as turbidity measurement, dynamic light scattering, Raleigh scattering, ThT fluorescence, intrinsic fluorescence, far-UV CD and atomic force microscopy. Sarkosyl was unable to induce aggregation in HEWL at pH 13.0 as confirmed by turbidity and RLS measurements. HEWL forms larger amyloid fibrils in the presence of 1.6 mM of sarkosyl. The spectroscopic, microscopic and molecular docking data suggest that the negatively charged carboxylate group and 12-carbon hydrophobic tail of sarkosyl stimulate amyloid fibril formation in HEWL via electrostatic and hydrophobic interaction. This study leads to new insight into the process of suppression of fibrillogenesis in HEWL which can be prevented by designing ligands that can retard the electrostatic and hydrophobic interaction between sarkosyl and HEWL.
Keywords:sarkosyl  surfactant  hen egg white lysozyme  protein aggregation  amyloid fibril formation and ThT
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号