期刊
NPJ COMPUTATIONAL MATERIALS
卷 6, 期 1, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41524-020-0288-7
关键词
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资金
- US Department of Energy, Office of Science, Office of Basic Energy Sciences, as part of the Energy Frontier Research Centers program: CSSAS, The Center for the Science of Synthesis Across Scales [DE-SC0019288]
- National Institute of Health [R21 A126113]
- University of Washington
- NSF MRI program [CHE-1624430]
Titania (TiO2) is used extensively in biomedical applications; efforts to boost the biocompatibility of TiO2 include coating it with the titania binding hexamer, RKLPDA. To understand the binding mechanism of this peptide, we employ molecular dynamics simulations enhanced by metadynamics to study three amino acids present in the peptide-arginine (R), lysine (K), and aspartate (D), on four TiO2 variants that have different degrees of surface hydroxyl groups. We find that binding is a function of both sidechain charge and structure, with R binding to all four surfaces, whereas the affinity of K and D is dependent on the distribution of hydroxyl groups. Informed by this, we study the binding of the titania binding hexamer and dodecamer (RKLPDAPGMHTW) on two of the four surfaces, and we see strong correlations between the binding free energy and the primary binding residues, in agreement with prior experiments and simulations. We propose that the discrepancies observed in prior work stem from distribution of surface hydroxyl groups that may be difficult to precisely control on the TiO2 interface.
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