期刊
APPLIED SURFACE SCIENCE
卷 384, 期 -, 页码 36-44出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.apsusc.2016.05.014
关键词
Nanostructure; Protein adsorption; Rutile; Molecular dynamics simulation
类别
资金
- National Natural Science Foundation of China [51201050]
- Self-Planned Task of State Key Laboratory of Robotics and System (HIT) [SKLRS201605C]
- Fundamental Research Funds for the Central Universities [AUGA5710058415]
- Program of Introducing Talents of Discipline to Universities [B07018]
- Office of Science of the U.S. Department of Energy [DE-ACO2-05CH11231]
- U.S. Department of Energy (DOE), Office of Basic Energy Sciences, Geoscience Research Program [ERKCC72]
- DOE by UT Battelle, LLC [DE-AC05-000R22725]
To investigate the topographical dependency of protein adsorption, molecular dynamics simulations were employed to describe the adsorption behavior of the tenth type-III module of fibronectin (FN-III10) on nanostructured rutile (110) surfaces. The results indicated that the residence time of adsorbed FN-III10 largely relied on its binding mode (direct or indirect) with the substrate and the region for protein migration on the periphery (protrusion) or in the interior (cavity or groove) of nanostructures. In the direct binding mode, FN-III10 molecules were found to be 'trapped' at the anchoring sites of rutile surface, or even penetrate deep into the interior of nanostructures, regardless of the presented geometrical features. In the indirect binding mode, FN-III10 molecules were indirectly connected to the substrate via a hydrogen-bond network (linking FN-III10 and interfacial hydrations). The facets created by nanostructures, which exerted restraints on protein migration, were suggested to play an important role in the stability of indirect FN-III10-rutile binding. However, a doubly unfavorable situation-indirect FN-III10-rutile connections bridged by a handful of mediating waters and few constraints on movement of protein provided by nanostructures-would result in an early desorption of protein. (C) 2016 Elsevier B.V. All rights reserved.
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