化学
对接(动物)
氢键
分子动力学
组氨酸
Zeta电位
肌原纤维
溶解度
结晶学
立体化学
生物物理学
计算化学
物理化学
分子
有机化学
生物化学
酶
化学工程
纳米颗粒
护理部
生物
工程类
医学
作者
Wei Wu,Qixing Jiang,Pei Gao,Dawei Yu,Peipei Yu,Wenshui Xia
标识
DOI:10.1016/j.ijbiomac.2023.126820
摘要
The effects of the L-hisdine (L-His)-assisted ultrasound on physicochemical characteristics and conformation of myofibrillar protein (MP) under reduced-salt condition were investigated using spectroscopic analysis, and the binding mechanism between L-His and MP was further elucidated through molecular docking and molecular dynamics (MD) simulations. UV second derivative spectra and intrinsic Try fluorescence spectra revealed that L-His formed a complex with MP and altered the microenvironment of MP. After L-His-assisted ultrasound treatment, MP showed smaller particle size, higher solubility, and more uniform atomic force microscopy image due to the decrease of α-helix content and the subsequent increase in zeta potential, active sulfhydryl content, and surface hydrophobicity. Molecular docking and MD simulations demonstrated the optimal docking pose (minimum binding affinity of -6.78 kcal/mol) and revealed hydrophobic interactions and hydrogen bonds as the main interaction forces between L-His and MP, with several residues (ILE-464, ILE-480, THR-483, ASN-484, GLY-466, ASP-463, PHE-246) identified as binding sites.
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