期刊
ACS OMEGA
卷 5, 期 49, 页码 32051-32058出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsomega.0c05080
关键词
-
资金
- National Research Foundation of Korea (NRF) - Ministry of Science and ICT [2020M2D8A206983011]
- Basic Science Research Program through the National Research Foundation of Korea [2017R1A2B3009135]
Nanotubes have been considered as promising candidates for protein delivery purposes due to distinct features such as their large enough volume of cavity to encapsulate the protein, providing the sustain and target release. Moreover, possessing the properties of suitable cell viabilities, and biocompatibility on the wide range of cell lines as a result of structural stability, chemical inertness, and noncovalent wrapping ability, boron nitride nanotubes (BNNTs) have caught further attention as protein nanocarriers. However, to assess the encapsulation process of the protein into the BNNT, it is vital to comprehend the protein-BNNT interaction. In the present work, the self-insertion process of the protein SmtA, metallothionein, into the BNNT has been verified by means of the molecular dynamics (MD) simulation under NPT ensemble. It was revealed that the protein was self-inserted into the BNNT through the protein-BNNT van der Waals (vdW) interaction, which descended and reached the average value of -189.63 kcal.mol(-1) at 15 ns of the simulation time. The potential mean force (PMF) profile of the encapsulated protein with increasing trend, which was obtained via the pulling process unraveled that the encapsulation of the protein into the BNNT cavity proceeded spontaneously and the self-inserted protein had reasonable stability. Moreover, due to the strong hydrogen interactions between the nitrogen atoms of BNNT and hydrogen atoms of SmtA, there was no evidence of an energy barrier in the vicinity of the BNNT entrance, which resulted in the rapid adsorption of this protein into the BNNT.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据