Revealing the regulation of water dipole potential to aggregation of amyloid-β42 at chiral interface by surface-enhanced infrared absorption spectroscopy
作者机构:State Key Laboratory of Electroanalytical ChemistryChangchun Institute of Applied ChemistryChinese Academy of SciencesChangchunChina School of Applied Chemistry and EngineeringUniversity of Science and Technology of ChinaHefeiChina Research Center for Analytical ScienceCollege of ChemistryNankai UniversityTianjinChina
出 版 物:《Aggregate》 (聚集体(英文))
年 卷 期:2024年第5卷第5期
页 面:454-464页
核心收录:
学科分类:081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学]
基 金:National Key R&D Program of China,Grant/Award Number:2022YFE0113000 National Science Fund for Distinguished Young Scholars,Grant/Award Number:22025406
主 题:amyloid-β42 chiral interface surface-enhanced infrared absorption spectroscopy
摘 要:Surface chirality plays an important role in determining the biological effect,but the molecular nature beyond stereoselectivity is still ***,through surface-enhanced infrared absorption spectroscopy,electrochemistry,and theoretical simulations,we found diasteromeric monolayers induced by assembled density on chiral gold nanofilm and identified the positive contribution of water dipole poten-tial at chiral interface and their different interfacial interactions,which result in a difference both in the positive dipoles of interfacial water compensating the negative surface potential of the SAM and in the hindrance effect of interface dehydration,thereby regulating the interaction between amyloid-βpeptide(Aβ)and N-isobutyryl-cysteine(NIBC).Water on L-NIBC interface which shows stronger positive dipole potential weakens the negative surface potential,but its local weak binding to the isopropyl group facilitates hydrophobic interaction between Aβ42 and L-NIBC and resultedfiber ***,electrostatic interaction between Aβ42 and D-NIBC induces spherical ***findings provide new insight into molecular nature of chirality-regulated biological effect.