Computational studies of the binding mechanisms of fullerenes to human serum albumin
Fullerene and its derivatives show promising prospects for applications in a vast array of biological systems.A key aspect concerning their biomedical applications is how they interact with proteins from molecular levels,which is still poorly understood.In the current study,we investigated the structural and thermodynamic basis of the interactions between two pharmacologically relevant fullerene derivatives and human serum albumin(HSA)using molecular docking,molecular dynamics simulations,and binding free energy calculations.Our results demonstrate that fullerenes steadily bind with HSA at the interfacial cavity formed by subdomains ⅡA and ⅢA,In agreement with available experimental data,our simulations show that the global structure of HSA becomes more compact in the presence of fullerene.while local structural dynamics of the binding cavity behaves diversely depending on the chemical properties of bound fullerenes.Binding free energy calculations confirmed that the interactions between fullerenes and HSA are dominantly stabilized by van der Waals forces and they Anther allowed the identification of key residues involved in fullerene binding.The structural and energetic insights obtained from this work may help for the development of fullerene-based drug delivery devices and therapeutic agents with improved biological profile.
Fullerene Human serum albumin Molecular simulation
Jinyu Li Lizhi Jiang Xiaolei Zhu
State Key Laboratory of Materials-Oriented Chemical Engineering.College of Chemistry and Chemical En State Key Laboratory of Materials-Oriented Chemical Engineering.College of Chemistry and Chemical En State Key Laboratory of Materials-Oriented Chemical Engineering.College of Chemistry and Chemical En
国内会议
大连
英文
157-165
2016-09-24（万方平台首次上网日期，不代表论文的发表时间）